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PDBsum entry 1aui

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
1aui
Jmol PyMol
Contents
Protein chains
378 a.a. *
165 a.a. *
Metals
_FE
_CA ×4
_ZN
Waters ×436
* Residue conservation analysis
PDB id:
1aui
Name: Hydrolase
Title: Human calcineurin heterodimer
Structure: Serine/threonine phosphatase 2b. Chain: a. Synonym: calcineurin. Engineered: yes. Serine/threonine phosphatase 2b. Chain: b. Synonym: calcineurin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.187    
Authors: C.R.Kissinger,H.E.Parge,D.R.Knighton,L.A.Pelletier,C.T.Lewis A.Tempczyk,J.E.Villafranca
Key ref: C.R.Kissinger et al. (1995). Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature, 378, 641-644. PubMed id: 8524402
Date:
27-Aug-97     Release date:   03-Dec-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q08209  (PP2BA_HUMAN) -  Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Seq:
Struc:
 
Seq:
Struc:
521 a.a.
378 a.a.*
Protein chain
Pfam   ArchSchema ?
P63098  (CANB1_HUMAN) -  Calcineurin subunit B type 1
Seq:
Struc:
170 a.a.
165 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 14 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.1.3.16  - Protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [a protein]-serine/threonine phosphate + H2O = [a protein]- serine/threonine + phosphate
[a protein]-serine/threonine phosphate
+ H(2)O
= [a protein]- serine/threonine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   11 terms 
  Biological process     negative regulation of chromatin binding   41 terms 
  Biochemical function     protein binding     15 terms  

 

 
    Key reference    
 
 
Nature 378:641-644 (1995)
PubMed id: 8524402  
 
 
Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex.
C.R.Kissinger, H.E.Parge, D.R.Knighton, C.T.Lewis, L.A.Pelletier, A.Tempczyk, V.J.Kalish, K.D.Tucker, R.E.Showalter, E.W.Moomaw.
 
  ABSTRACT  
 
Calcineurin (CaN) is a calcium- and calmodulin-dependent protein serine/threonine phosphate which is critical for several important cellular processes, including T-cell activation. CaN is the target of the immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after forming complexes with cytoplasmic binding proteins (cyclophilin and FKBP12, respectively). We report here the crystal structures of full-length human CaN at 2.1 A resolution and of the complex of human CaN with FKBP12-FK506 at 3.5 A resolution. In the native CaN structure, an auto-inhibitory element binds at the Zn/Fe-containing active site. The metal-site geometry and active-site water structure suggest a catalytic mechanism involving nucleophilic attack on the substrate phosphate by a metal-activated water molecule. In the FKBP12-FK506-CaN complex, the auto-inhibitory element is displaced from the active site. The site of binding of FKBP12-FK506 appears to be shared by other non-competitive inhibitors of calcineurin, including a natural anchoring protein.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22173432 Y.Pommier, and C.Marchand (2012).
Interfacial inhibitors: targeting macromolecular complexes.
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21295458 A.Mukherjee, and C.Soto (2011).
Role of calcineurin in neurodegeneration produced by misfolded proteins and endoplasmic reticulum stress.
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20934451 D.W.Song, J.G.Lee, H.S.Youn, S.H.Eom, and d.o. .H.Kim (2011).
Ryanodine receptor assembly: A novel systems biology approach to 3D mapping.
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21261611 G.Terukina, Y.Yoshida, and N.Takahashi (2011).
Peptidyl-prolyl cis-trans isomerase xFKBP1B induces ectopic secondary axis and is involved in eye formation during Xenopus embryogenesis.
  Dev Growth Differ, 53, 55-68.  
21115349 H.Li, A.Rao, and P.G.Hogan (2011).
Interaction of calcineurin with substrates and targeting proteins.
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21287611 S.E.O'Donnell, L.Yu, C.A.Fowler, and M.A.Shea (2011).
Recognition of β-calcineurin by the domains of calmodulin: Thermodynamic and structural evidence for distinct roles.
  Proteins, 79, 765-786.  
21288162 S.R.Pereira, V.T.Vasconcelos, and A.Antunes (2011).
The phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring toxins.
  Crit Rev Toxicol, 41, 83.  
19967549 K.Kurji, and R.K.Sharma (2010).
Potential role of calcineurin in pathogenic conditions.
  Mol Cell Biochem, 338, 133-141.  
20552635 Q.Chen, W.Wu, J.Li, and Q.Wei (2010).
The polarity of the amino acid residue 118 of calcineurin B is closely linked to calcineurin enzyme activity.
  IUBMB Life, 62, 561-567.  
20572013 R.Alag, I.A.Qureshi, N.Bharatham, J.Shin, J.Lescar, and H.S.Yoon (2010).
NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.
  Protein Sci, 19, 1577-1586.
PDB code: 3ihz
21048386 Y.Amasaki (2010).
[Calcineurin inhibitors and calcineurin-NFAT system].
  Nihon Rinsho Meneki Gakkai Kaishi, 33, 249-261.  
19823697 A.Agbas, and J.Moskovitz (2009).
The Role of Methionine Oxidation/Reduction in the Regulation of Immune Response.
  Curr Signal Transduct Ther, 4, 46-50.  
19716552 A.Bahi, Y.S.Mineur, and M.R.Picciotto (2009).
Blockade of protein phosphatase 2B activity in the amygdala increases anxiety- and depression-like behaviors in mice.
  Biol Psychiatry, 66, 1139-1146.  
19531490 A.Khromov, N.Choudhury, A.S.Stevenson, A.V.Somlyo, and M.Eto (2009).
Phosphorylation-dependent Autoinhibition of Myosin Light Chain Phosphatase Accounts for Ca2+ Sensitization Force of Smooth Muscle Contraction.
  J Biol Chem, 284, 21569-21579.  
19285944 A.Rodríguez, J.Roy, S.Martínez-Martínez, M.D.López-Maderuelo, P.Niño-Moreno, L.Ortí, D.Pantoja-Uceda, A.Pineda-Lucena, M.S.Cyert, and J.M.Redondo (2009).
A conserved docking surface on calcineurin mediates interaction with substrates and immunosuppressants.
  Mol Cell, 33, 616-626.  
19597536 B.He, K.Wang, Y.Liu, B.Xue, V.N.Uversky, and A.K.Dunker (2009).
Predicting intrinsic disorder in proteins: an overview.
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19387497 E.I.Graziani (2009).
Recent advances in the chemistry, biosynthesis and pharmacology of rapamycin analogs.
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19162087 G.Taglialatela, D.Hogan, W.R.Zhang, and K.T.Dineley (2009).
Intermediate- and long-term recognition memory deficits in Tg2576 mice are reversed with acute calcineurin inhibition.
  Behav Brain Res, 200, 95-99.  
19299564 J.L.McConnell, and B.E.Wadzinski (2009).
Targeting protein serine/threonine phosphatases for drug development.
  Mol Pharmacol, 75, 1249-1261.  
19290928 J.O.Liu (2009).
Calmodulin-dependent phosphatase, kinases, and transcriptional corepressors involved in T-cell activation.
  Immunol Rev, 228, 184-198.  
19277847 J.S.Woo, J.H.Hwang, J.K.Ko, d.o. .H.Kim, J.Ma, and E.H.Lee (2009).
Glutamate at position 227 of junctophilin-2 is involved in binding to TRPC3.
  Mol Cell Biochem, 328, 25-32.  
19052845 K.O.Yaykasli, T.Oohashi, S.Hirohata, O.F.Hatipoglu, K.Inagawa, K.Demircan, and Y.Ninomiya (2009).
ADAMTS9 activation by interleukin 1 beta via NFATc1 in OUMS-27 chondrosarcoma cells and in human chondrocytes.
  Mol Cell Biochem, 323, 69-79.  
  19241373 M.Pierechod, A.Nowak, A.Saari, E.Purta, J.M.Bujnicki, and I.Konieczny (2009).
Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system.
  Protein Sci, 18, 637-649.  
19860902 M.Sieber, and R.Baumgrass (2009).
Novel inhibitors of the calcineurin/NFATc hub - alternatives to CsA and FK506?
  Cell Commun Signal, 7, 25.  
19701943 S.Mori, R.Iwaoka, M.Eto, and S.Y.Ohki (2009).
Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1.
  Proteins, 77, 732-735.
PDB code: 2kjy
19852730 S.Ryeom, K.H.Baek, and A.Zaslavsky (2009).
Down's syndrome: protection against cancer and the therapeutic potential of DSCR1.
  Future Oncol, 5, 1185-1188.  
18925649 X.J.Xie, W.Huang, C.Z.Xue, and Q.Wei (2009).
The nonconserved N-terminus of protein phosphatase 2B confers its properties to protein phosphatase 1.
  IUBMB Life, 61, 178-183.  
19242655 X.J.Xie, W.Huang, C.Z.Xue, and Q.Wei (2009).
The N-terminal domain influences the structure and property of protein phosphatase 1.
  Mol Cell Biochem, 327, 241-246.  
19558332 Y.Ren, Z.X.Wang, and Q.Wei (2009).
Mechanism of activation of Saccharomyces cerevisiae calcineurin by Mn2+.
  Biol Chem, 390, 1155-1162.  
19879837 Y.Shi (2009).
Serine/threonine phosphatases: mechanism through structure.
  Cell, 139, 468-484.  
18162540 B.Ruan, K.Pong, F.Jow, M.Bowlby, R.A.Crozier, D.Liu, S.Liang, Y.Chen, M.L.Mercado, X.Feng, F.Bennett, D.von Schack, L.McDonald, M.M.Zaleska, A.Wood, P.H.Reinhart, R.L.Magolda, J.Skotnicki, M.N.Pangalos, F.E.Koehn, G.T.Carter, M.Abou-Gharbia, and E.I.Graziani (2008).
Binding of rapamycin analogs to calcium channels and FKBP52 contributes to their neuroprotective activities.
  Proc Natl Acad Sci U S A, 105, 33-38.  
18488168 B.Wang, P.Zhang, and Q.Wei (2008).
Recent progress on the structure of Ser/Thr protein phosphatases.
  Sci China C Life Sci, 51, 487-494.  
18798625 C.McWhirter, E.A.Lund, E.A.Tanifum, G.Feng, Q.I.Sheikh, A.C.Hengge, and N.H.Williams (2008).
Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzyme.
  J Am Chem Soc, 130, 13673-13682.  
18065652 J.Stie, and D.Fox (2008).
Calcineurin regulation in fungi and beyond.
  Eukaryot Cell, 7, 177-186.  
18771593 K.S.Hadler, T.Huber, A.I.Cassady, J.Weber, J.Robinson, A.Burrows, G.Kelly, L.W.Guddat, D.A.Hume, G.Schenk, and J.U.Flanagan (2008).
Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?
  BMC Res Notes, 1, 78.  
18216259 M.A.Fischbach, C.T.Walsh, and J.Clardy (2008).
The evolution of gene collectives: How natural selection drives chemical innovation.
  Proc Natl Acad Sci U S A, 105, 4601-4608.  
18296644 M.Koutmos, R.Pejchal, T.M.Bomer, R.G.Matthews, J.L.Smith, and M.L.Ludwig (2008).
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
  Proc Natl Acad Sci U S A, 105, 3286-3291.
PDB codes: 3bof 3bol 3bq5 3bq6
18384083 Q.Ye, H.Wang, J.Zheng, Q.Wei, and Z.Jia (2008).
The complex structure of calmodulin bound to a calcineurin peptide.
  Proteins, 73, 19-27.
PDB code: 2r28
18186485 R.Worch, and R.Stolarski (2008).
Stacking efficiency and flexibility analysis of aromatic amino acids in cap-binding proteins.
  Proteins, 71, 2026-2037.  
  18765925 T.Oda, H.Hashimoto, N.Kuwabara, K.Hayashi, C.Kojima, T.Kawasaki, K.Shimamoto, M.Sato, and T.Shimizu (2008).
Crystallographic characterization of the N-terminal domain of a plant NADPH oxidase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 867-869.  
18296442 X.Shen, H.Li, Y.Ou, W.Tao, A.Dong, J.Kong, C.Ji, and S.Yu (2008).
The secondary structure of calcineurin regulatory region and conformational change induced by calcium/calmodulin binding.
  J Biol Chem, 283, 11407-11413.  
17284813 A.J.Bortoluzzi, A.Neves, and N.A.Rey (2007).
2-{[Bis(2-pyridylmethyl)amino]methyl}-6-[(2-hydroxyanilino)methyl]-4-methylphenol: a novel binucleating asymmetric ligand as a precursor to synthetic models for metalloenzymes.
  Acta Crystallogr C, 63, o84-o86.  
17391014 H.Xie, S.Vucetic, L.M.Iakoucheva, C.J.Oldfield, A.K.Dunker, V.N.Uversky, and Z.Obradovic (2007).
Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.
  J Proteome Res, 6, 1882-1898.  
17614939 H.Yu, T.J.van Berkel, and E.A.Biessen (2007).
Therapeutic potential of VIVIT, a selective peptide inhibitor of nuclear factor of activated T cells, in cardiovascular disorders.
  Cardiovasc Drug Rev, 25, 175-187.  
17502104 K.Takeuchi, M.H.Roehrl, Z.Y.Sun, and G.Wagner (2007).
Structure of the calcineurin-NFAT complex: defining a T cell activation switch using solution NMR and crystal coordinates.
  Structure, 15, 587-597.
PDB code: 2jog
17499048 M.J.Sánchez-Barrena, H.Fujii, I.Angulo, M.Martínez-Ripoll, J.K.Zhu, and A.Albert (2007).
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3.
  Mol Cell, 26, 427-435.
PDB code: 2ehb
17050540 M.Mishima, S.Wakabayashi, and C.Kojima (2007).
Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1.
  J Biol Chem, 282, 2741-2751.
PDB code: 2e30
17324936 M.Saeki, Y.Irie, L.Ni, Y.Itsuki, Y.Terao, S.Kawabata, and Y.Kamisaki (2007).
Calcineurin potentiates the activation of procaspase-3 by accelerating its proteolytic maturation.
  J Biol Chem, 282, 11786-11794.  
17694572 M.Sieber, M.Karanik, C.Brandt, C.Blex, M.Podtschaske, F.Erdmann, R.Rost, E.Serfling, J.Liebscher, M.Pätzel, A.Radbruch, G.Fischer, and R.Baumgrass (2007).
Inhibition of calcineurin-NFAT signaling by the pyrazolopyrimidine compound NCI3.
  Eur J Immunol, 37, 2617-2626.  
17636256 T.D.Hurley, J.Yang, L.Zhang, K.D.Goodwin, Q.Zou, M.Cortese, A.K.Dunker, and A.A.DePaoli-Roach (2007).
Structural basis for regulation of protein phosphatase 1 by inhibitor-2.
  J Biol Chem, 282, 28874-28883.
PDB codes: 2o8a 2o8g
17505522 W.J.Steinbach, J.L.Reedy, R.A.Cramer, J.R.Perfect, and J.Heitman (2007).
Harnessing calcineurin as a novel anti-infective agent against invasive fungal infections.
  Nat Rev Microbiol, 5, 418-430.  
16639748 A.M.Tokheim, and B.L.Martin (2006).
Association of calcineurin with mitochondrial proteins.
  Proteins, 64, 28-33.  
16505102 C.Marchand, S.Antony, K.W.Kohn, M.Cushman, A.Ioanoviciu, B.L.Staker, A.B.Burgin, L.Stewart, and Y.Pommier (2006).
A novel norindenoisoquinoline structure reveals a common interfacial inhibitor paradigm for ternary trapping of the topoisomerase I-DNA covalent complex.
  Mol Cancer Ther, 5, 287-295.  
16705489 J.D.Hoekman, A.M.Tokheim, D.J.Spannaus-Martin, and B.L.Martin (2006).
Molecular modeling of the calmodulin binding region of calcineurin.
  Protein J, 25, 175-182.  
16844742 J.Wang, Y.Deng, and B.Roux (2006).
Absolute binding free energy calculations using molecular dynamics simulations with restraining potentials.
  Biophys J, 91, 2798-2814.  
16805817 N.Shioda, S.Moriguchi, Y.Shirasaki, and K.Fukunaga (2006).
Generation of constitutively active calcineurin by calpain contributes to delayed neuronal death following mouse brain ischemia.
  J Neurochem, 98, 310-320.  
  18404474 N.Sträter (2006).
Ecto-5'-nucleotidase: Structure function relationships.
  Purinergic Signal, 2, 343-350.  
17015448 O.H.Weiergräber, I.I.Senin, E.Y.Zernii, V.A.Churumova, N.A.Kovaleva, A.A.Nazipova, S.E.Permyakov, E.A.Permyakov, P.P.Philippov, J.Granzin, and K.W.Koch (2006).
Tuning of a neuronal calcium sensor.
  J Biol Chem, 281, 37594-37602.
PDB code: 2het
16493654 P.Radivojac, S.Vucetic, T.R.O'Connor, V.N.Uversky, Z.Obradovic, and A.K.Dunker (2006).
Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition.
  Proteins, 63, 398-410.  
17001103 R.M.Esnouf, R.Hamer, J.L.Sussman, I.Silman, D.Trudgian, Z.R.Yang, and J.Prilusky (2006).
Honing the in silico toolkit for detecting protein disorder.
  Acta Crystallogr D Biol Crystallogr, 62, 1260-1266.  
17081120 X.J.Xie, C.Z.Xue, W.Huang, D.Y.Yu, and Q.Wei (2006).
The beta12-beta13 loop is a key regulatory element for the activity and properties of the catalytic domain of protein phosphatase 1 and 2B.
  Biol Chem, 387, 1461-1467.  
16710297 Y.B.Ammar, S.Takeda, T.Hisamitsu, H.Mori, and S.Wakabayashi (2006).
Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation.
  EMBO J, 25, 2315-2325.
PDB code: 2bec
16876893 Y.Cheng, T.LeGall, C.J.Oldfield, J.P.Mueller, Y.Y.Van, P.Romero, M.S.Cortese, V.N.Uversky, and A.K.Dunker (2006).
Rational drug design via intrinsically disordered protein.
  Trends Biotechnol, 24, 435-442.  
16218947 A.K.Dunker, M.S.Cortese, P.Romero, L.M.Iakoucheva, and V.N.Uversky (2005).
Flexible nets. The roles of intrinsic disorder in protein interaction networks.
  FEBS J, 272, 5129-5148.  
15832371 A.Lakshmikuttyamma, P.Selvakumar, R.Kanthan, S.C.Kanthan, and R.K.Sharma (2005).
Increased expression of calcineurin in human colorectal adenocarcinomas.
  J Cell Biochem, 95, 731-739.  
15671033 A.Rodríguez, S.Martínez-Martínez, M.D.López-Maderuelo, I.Ortega-Pérez, and J.M.Redondo (2005).
The linker region joining the catalytic and the regulatory domains of CnA is essential for binding to NFAT.
  J Biol Chem, 280, 9980-9984.  
15845546 B.Adams, A.Musiyenko, R.Kumar, and S.Barik (2005).
A novel class of dual-family immunophilins.
  J Biol Chem, 280, 24308-24314.  
16131541 B.Chan, G.Greenan, F.McKeon, and T.Ellenberger (2005).
Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo.
  Proc Natl Acad Sci U S A, 102, 13075-13080.  
15788412 D.Wang, M.Guo, Z.Liang, J.Fan, Z.Zhu, J.Zang, Z.Zhu, X.Li, M.Teng, L.Niu, Y.Dong, and P.Liu (2005).
Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites.
  J Biol Chem, 280, 22962-22967.
PDB code: 1w24
16096803 E.G.Funhoff, T.E.de Jongh, and B.A.Averill (2005).
Direct observation of multiple protonation states in recombinant human purple acid phosphatase.
  J Biol Inorg Chem, 10, 550-563.  
15955057 E.G.Funhoff, Y.Wang, G.Andersson, and B.A.Averill (2005).
Substrate positioning by His92 is important in catalysis by purple acid phosphatase.
  FEBS J, 272, 2968-2977.  
16177924 J.Hu, X.Yang, and K.Wang (2005).
La3+ stimulate the activity of calcineurin in two different ways.
  J Biol Inorg Chem, 10, 704-711.  
16113294 J.R.Blankenship, and J.Heitman (2005).
Calcineurin is required for Candida albicans to survive calcium stress in serum.
  Infect Immun, 73, 5767-5774.  
15577939 J.Yang, S.M.Roe, M.J.Cliff, M.A.Williams, J.E.Ladbury, P.T.Cohen, and D.Barford (2005).
Molecular basis for TPR domain-mediated regulation of protein phosphatase 5.
  EMBO J, 24, 1.
PDB code: 1wao
16148011 S.Kang, H.Li, A.Rao, and P.G.Hogan (2005).
Inhibition of the calcineurin-NFAT interaction by small organic molecules reflects binding at an allosteric site.
  J Biol Chem, 280, 37698-37706.  
15657058 S.O.Sio, T.Suehiro, R.Sugiura, M.Takeuchi, H.Mukai, and T.Kuno (2005).
The role of the regulatory subunit of fission yeast calcineurin for in vivo activity and its relevance to FK506 sensitivity.
  J Biol Chem, 280, 12231-12238.  
15987692 Y.Naoe, K.Arita, H.Hashimoto, H.Kanazawa, M.Sato, and T.Shimizu (2005).
Structural characterization of calcineurin B homologous protein 1.
  J Biol Chem, 280, 32372-32378.
PDB code: 2ct9
  16511110 Y.Naoe, K.Arita, H.Hashimoto, H.Kanazawa, M.Sato, and T.Shimizu (2005).
Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 612-613.  
15749159 Y.Pommier, and J.Cherfils (2005).
Interfacial inhibition of macromolecular interactions: nature's paradigm for drug discovery.
  Trends Pharmacol Sci, 26, 138-145.  
15947016 Z.R.Yang, R.Thomson, P.McNeil, and R.M.Esnouf (2005).
RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins.
  Bioinformatics, 21, 3369-3376.  
15555063 A.V.Andreeva, and M.A.Kutuzov (2004).
Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes.
  BMC Evol Biol, 4, 47.  
15123671 H.Liu, M.Holm, X.Q.Xie, M.Wolf-Watz, and T.Grundström (2004).
AML1/Runx1 recruits calcineurin to regulate granulocyte macrophage colony-stimulating factor by Ets1 activation.
  J Biol Chem, 279, 29398-29408.  
15005855 H.Mitsuyama, F.Kambe, R.Murakami, X.Cao, N.Ishiguro, and H.Seo (2004).
Calcium signaling pathway involving calcineurin regulates interleukin-8 gene expression through activation of NF-kappaB in human osteoblast-like cells.
  J Bone Miner Res, 19, 671-679.  
15164081 M.Terrak, F.Kerff, K.Langsetmo, T.Tao, and R.Dominguez (2004).
Structural basis of protein phosphatase 1 regulation.
  Nature, 429, 780-784.
PDB code: 1s70
14583619 R.Baumgrass, Y.Zhang, F.Erdmann, A.Thiel, M.Weiwad, A.Radbruch, and G.Fischer (2004).
Substitution in position 3 of cyclosporin A abolishes the cyclophilin-mediated gain-of-function mechanism but not immunosuppression.
  J Biol Chem, 279, 2470-2479.  
15230980 R.Kumar, A.Musiyenko, A.Oldenburg, B.Adams, and S.Barik (2004).
Post-translational generation of constitutively active cores from larger phosphatases in the malaria parasite, Plasmodium falciparum: implications for proteomics.
  BMC Mol Biol, 5, 6.  
15381847 S.Barik (2004).
When proteome meets genome: the alpha helix and the beta strand of proteins are eschewed by mRNA splice junctions and may define the minimal indivisible modules of protein architecture.
  J Biosci, 29, 261-273.  
15128743 S.Chen, A.F.Yakunin, E.Kuznetsova, D.Busso, R.Pufan, M.Proudfoot, R.Kim, and S.H.Kim (2004).
Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii.
  J Biol Chem, 279, 31854-31862.
PDB codes: 1s3l 1s3m 1s3n
14711669 S.Y.McLoughlin, C.Jackson, J.W.Liu, and D.L.Ollis (2004).
Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source.
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14704353 Y.Shen, X.F.Tang, H.Yokoyama, E.Matsui, and I.Matsui (2004).
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15117942 Y.Terui, N.Saad, S.Jia, F.McKeon, and J.Yuan (2004).
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12598656 A.J.Stewart, C.A.Blindauer, S.Berezenko, D.Sleep, and P.J.Sadler (2003).
Interdomain zinc site on human albumin.
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14669985 B.Xiang, P.Liu, G.Jiang, K.Zou, F.Yi, S.Yang, and Q.Wei (2003).
The catalytically active domain in the A subunit of calcineurin.
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12604527 C.Onyewu, J.R.Blankenship, M.Del Poeta, and J.Heitman (2003).
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14557260 C.Zambonelli, M.Casali, and M.F.Roberts (2003).
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12725927 E.M.Del Aguila, J.T.Silva, and V.M.Paschoalin (2003).
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14581219 F.Sun, P.Li, Y.Ding, L.Wang, M.Bartlam, C.Shu, B.Shen, H.Jiang, S.Li, and Z.Rao (2003).
Design and structure-based study of new potential FKBP12 inhibitors.
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PDB codes: 1j4h 1j4i
14515992 G.Jiang, and Q.Wei (2003).
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12787506 I.A.Graef, F.Wang, F.Charron, L.Chen, J.Neilson, M.Tessier-Lavigne, and G.R.Crabtree (2003).
Neurotrophins and netrins require calcineurin/NFAT signaling to stimulate outgrowth of embryonic axons.
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12777780 M.Nagae, A.Nozawa, N.Koizumi, H.Sano, H.Hashimoto, M.Sato, and T.Shimizu (2003).
Crystallization and preliminary X-ray characterization of a novel calcium-binding protein AtCBL2 from Arabidopsis thaliana.
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The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana.
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12740046 N.Rekha, and N.Srinivasan (2003).
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12874277 O.Mignen, J.L.Thompson, and T.J.Shuttleworth (2003).
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11879652 A.Kuhara, H.Inada, I.Katsura, and I.Mori (2002).
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12000771 K.J.Babinski, S.J.Kanjilal, and C.R.Raetz (2002).
Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene.
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PDB code: 1mf8
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11774230 G.R.Marshall (2001).
Peptide interactions with G-protein coupled receptors.
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Potent inhibition of NFAT activation and T cell cytokine production by novel low molecular weight pyrazole compounds.
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Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1.
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PDB code: 1jk7
11344324 L.M.Iakoucheva, A.L.Kimzey, C.D.Masselon, J.E.Bruce, E.C.Garner, C.J.Brown, A.K.Dunker, R.D.Smith, and E.J.Ackerman (2001).
Identification of intrinsic order and disorder in the DNA repair protein XPA.
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Calcineurin activity is regulated both by redox compounds and by mutant familial amyotrophic lateral sclerosis-superoxide dismutase.
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10713512 C.C.Deivanayagam, M.Carson, A.Thotakura, S.V.Narayana, and R.S.Chodavarapu (2000).
Structure of FKBP12.6 in complex with rapamycin.
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PDB code: 1c9h
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Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics.
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Molecular modeling of the catalytic domain of serine/threonine phosphatase-1 with the Zn2+ and Mn2+ di-nuclear ion centers in the active site.
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Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies.
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PDB codes: 1dgu 1dgv
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A second calcineurin binding site on the NFAT regulatory domain.
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Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes.
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Identification of a novel region critical for calcineurin function in vivo and in vitro.
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Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+.
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Autoinhibition of endothelial nitric-oxide synthase. Identification of an electron transfer control element.
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Calcineurin. Structure, function, and inhibition.
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Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src).
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A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A.
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Interaction of bacteriophage lambda protein phosphatase with Mn(II): evidence for the formation of a [Mn(II)]2 cluster.
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Characterization of the inhibition of protein phosphatase-1 by DARPP-32 and inhibitor-2.
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Three amino acid residues determine selective binding of FK506-binding protein 12.6 to the cardiac ryanodine receptor.
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Tartrate-resistant bone acid phosphatase: large-scale production and purification of the recombinant enzyme, characterization, and crystallization.
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Genes for calcineurin B-like proteins in Arabidopsis are differentially regulated by stress signals.
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Stimulation of Elk1 transcriptional activity by mitogen-activated protein kinases is negatively regulated by protein phosphatase 2B (calcineurin).
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Signaling through calcium, calcineurin, and NF-AT in lymphocyte activation and development.
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Crystal structure of mammalian purple acid phosphatase.
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PDB code: 1ute
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High activity of the calcineurin A subunit with a V314 deletion.
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Antifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug action.
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Affinity modulation of small-molecule ligands by borrowing endogenous protein surfaces.
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Preparation and immunosuppressive activity of 32-(O)-acylated and 32-(O)-thioacylated analogues of ascomycin.
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Calcium-dependent and -independent interactions of the calmodulin-binding domain of cyclic nucleotide phosphodiesterase with calmodulin.
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X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
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AKAP79 inhibits calcineurin through a site distinct from the immunophilin-binding region.
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Inhibition of calcineurin by the tyrphostin class of tyrosine kinase inhibitors.
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Regulation of the calmodulin-stimulated protein phosphatase, calcineurin.
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The structure and mechanism of protein phosphatases: insights into catalysis and regulation.
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Two-site interaction of nuclear factor of activated T cells with activated calcineurin.
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Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT.
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Inhibitor-1 interaction domain that mediates the inhibition of protein phosphatase-1.
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Functional characterization and localization of protein phosphatase type 2C from Paramecium.
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Signal-transduction cascades as targets for therapeutic intervention by natural products.
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Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination.
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Cain, a novel physiologic protein inhibitor of calcineurin.
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Ga3+ as a functional substitute for Fe3+: preparation and characterization of the Ga3+Fe2+ and Ga3+Zn2+ forms of bovine spleen purple acid phosphatase.
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The activity of oxidized bovine spleen purple acid phosphatase is due to an Fe(III)Zn(II) 'impurity'.
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Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin.
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Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding.
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Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin.
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Isotope effect studies on the calcineurin phosphoryl-transfer reaction: transition state structure and effect of calmodulin and Mn2+.
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FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain.
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Overexpression and purification of human calcineurin alpha from Escherichia coli and assessment of catalytic functions of residues surrounding the binuclear metal center.
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The immunosuppressant FK506 and its nonimmunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein.
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Transcription factors of the NFAT family: regulation and function.
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Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding.
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Expression and function of calcineurin in the mammalian nephron: physiological roles, receptor signaling, and ion transport.
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Calcineurin regulation of synaptic function: from ion channels to transmitter release and gene transcription.
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Spectroscopic and enzymatic characterization of the active site dinuclear metal center of calcineurin: implications for a mechanistic role.
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Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1.
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Immunosuppressive agents in clinical trials in transplantation.
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Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C.
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Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and lambda protein phosphatase.
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Mutagenesis of the L7 loop connecting beta strands 12 and 13 of calcineurin: evidence for a structural role in activity changes.
  Biochemistry, 36, 7418-7424.  
  9003755 A.K.Das, N.R.Helps, P.T.Cohen, and D.Barford (1996).
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
  EMBO J, 15, 6798-6809.
PDB code: 1a6q
8994877 B.L.Stoddard, and K.E.Flick (1996).
Calcineurin-immunosuppressor complexes.
  Curr Opin Struct Biol, 6, 770-775.  
8987393 D.Barford (1996).
Molecular mechanisms of the protein serine/threonine phosphatases.
  Trends Biochem Sci, 21, 407-412.  
8768897 J.E.Villafranca, C.R.Kissinger, and H.E.Parge (1996).
Protein serine/threonine phosphatases.
  Curr Opin Biotechnol, 7, 397-402.  
8898189 J.M.Denu, J.A.Stuckey, M.A.Saper, and J.E.Dixon (1996).
Form and function in protein dephosphorylation.
  Cell, 87, 361-364.  
8702699 J.P.Raufman, J.Lin, and R.D.Raffaniello (1996).
Calcineurin mediates calcium-induced potentiation of adenylyl cyclase activity in dispersed chief cells from guinea pig stomach. Further evidence for cross-talk between signal transduction pathways that regulate pepsinogen secretion.
  J Biol Chem, 271, 19877-19882.  
8994885 M.A.Navia (1996).
Protein-drug complexes important for immunoregulation and organ transplantation.
  Curr Opin Struct Biol, 6, 838-847.  
8646534 M.B.Swindells, and M.Ikura (1996).
Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications binding IQ-motifs.
  Nat Struct Biol, 3, 501-504.  
8696978 M.Chytil, and G.L.Verdine (1996).
The Rel family of eukaryotic transcription factors.
  Curr Opin Struct Biol, 6, 91.  
9101762 P.Taylor, V.Mikol, J.Kallen, P.Burkhard, and M.D.Walkinshaw (1996).
Conformational polymorphism in peptidic and nonpeptidic drug molecules.
  Biopolymers, 40, 585-592.  
8798696 T.Ansai, L.C.Dupuy, and S.Barik (1996).
Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence.
  J Biol Chem, 271, 24401-24407.  
8909292 X.Wang, C.R.Randall, A.E.True, and L.Que (1996).
X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin.
  Biochemistry, 35, 13946-13954.  
8652512 Y.Zhao, and H.Ke (1996).
Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.
  Biochemistry, 35, 7362-7368.
PDB codes: 2cyh 3cyh 4cyh 5cyh
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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