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PDBsum entry 1f8a

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Isomerase PDB id
1f8a
Jmol
Contents
Protein chain
155 a.a. *
Ligands
TYR-SEP-PRO-THR-
SEP-PRO-SER
Waters ×152
* Residue conservation analysis
PDB id:
1f8a
Name: Isomerase
Title: Structural basis for the phosphoserine-proline recognition b ww domains
Structure: Peptidyl-prolyl cis-trans isomerase nima-interact chain: b. Synonym: pin1. Engineered: yes. Y(sep)pt(sep)s peptide. Chain: c. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: solid-phase peptide synthesis
Biol. unit: Dimer (from PQS)
Resolution:
1.84Å     R-factor:   0.231     R-free:   0.271
Authors: M.A.Verdecia,M.E.Bowman,K.P.Lu,T.Hunter,J.P.Noel
Key ref:
M.A.Verdecia et al. (2000). Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat Struct Biol, 7, 639-643. PubMed id: 10932246 DOI: 10.1038/77929
Date:
29-Jun-00     Release date:   23-Aug-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Seq:
Struc:
163 a.a.
155 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
Bound ligand (Het Group name = TYR)
matches with 41.18% similarity
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     midbody   5 terms 
  Biological process     negative regulation of cell motility   15 terms 
  Biochemical function     protein binding     7 terms  

 

 
    Added reference    
 
 
DOI no: 10.1038/77929 Nat Struct Biol 7:639-643 (2000)
PubMed id: 10932246  
 
 
Structural basis for phosphoserine-proline recognition by group IV WW domains.
M.A.Verdecia, M.E.Bowman, K.P.Lu, T.Hunter, J.P.Noel.
 
  ABSTRACT  
 
Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain connected by a flexible linker. To address the energetic and structural basis for WW domain recognition of phosphoserine (P.Ser)/phosphothreonine (P. Thr)- proline containing proteins, we report the energetic and structural analysis of a Pin1-phosphopeptide complex. The X-ray crystal structure of Pin1 bound to a doubly phosphorylated peptide (Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser) representing a heptad repeat of the RNA polymerase II large subunit's C-terminal domain (CTD), reveals the residues involved in the recognition of a single P.Ser side chain, the rings of two prolines, and the backbone of the CTD peptide. The side chains of neighboring Arg and Ser residues along with a backbone amide contribute to recognition of P.Ser. The lack of widespread conservation of the Arg and Ser residues responsible for P.Ser recognition in the WW domain family suggests that only a subset of WW domains can bind P.Ser-Pro in a similar fashion to that of Pin1.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Overall architecture of human Pin1. a, Ribbon representation of the Pin1 -CTD peptide complex. Residues 1 -5 of Pin1 are visible in the electron density maps but not shown here for clarity; residues 39 -50 are disordered. Apostrophes distinguish the WW domain colored purple from the PPIase domain colored blue. The CTD peptide backbone is yellow. Residues of the CTD peptide are labeled with primes. Atoms are colored according to type: carbon, light gray; nitrogen, blue; phosphorus, black; oxygen, red; sulfur, yellow. Dotted green lines depict hydrogen bonds. b, Ribbon representation of the Pin1 -PEG complex19. c, Stereo view of the SIGMAA weighted |2F[o] - F[c]| electron density map contoured at 1.0 around the Tyr 23-Trp 34 clamp.
Figure 2.
Figure 2. The Pin1 -CTD peptide binding interface. a, Ribbon diagram of the Pin1 WW domain bound to Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser depicted after a 90 rotation around a vertical axis from the view shown in Fig. 1a. This view is looking onto the concave WW domain peptide binding surface opposite the PPIase domain. The carbon atoms of the CTD peptide are colored gold to distinguish them from the WW domain side chain atoms. The water molecule mediating Tyr 23 -phosphate contacts is shown as a cyan sphere. Hydrogen bonds are shown as green dotted spheres. b, Molecular surface representation of the WW domain -peptide interface rendered after a slight rotation around the vertical axis from the view depicted in (a). The solvent accessible surface for the Pin1 WW domain residues was calculated in GRASP33, and the acidic and basic residues colored red and blue, respectively. c, Schematic and energetic view of the Pin1 -phosphopeptide complex. Pin1 residues are purple and CTD residues black. Residues participating in van der Waals contacts are highlighted with gold and the extended van der Waals surfaces appear as dotted gold curves. Hydrogen bonds are shown as dashed green lines. In the case of the S16H and W34H mutants, some of the apparent binding is likely being contributed by the PPIase domain. Residues are given in the single letter code. Values in parentheses represent deviations from theoretical binding isotherms.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 639-643) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Novel survivin mutant protects differentiated SK-N-SH human neuroblastoma cells from activated T-cell neurotoxicity.
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19291099 B.Wu, M.F.Rega, J.Wei, H.Yuan, R.Dahl, Z.Zhang, and M.Pellecchia (2009).
Discovery and binding studies on a series of novel Pin1 ligands.
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Prolyl isomerase Pin1 shares functional similarity with phosphorylated CTD interacting factor PCIF1 in vertebrate cells.
  Genes Cells, 14, 1105-1118.  
19639385 J.W.Peng, B.D.Wilson, and A.T.Namanja (2009).
Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance.
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Sequence determinants of thermodynamic stability in a WW domain--an all-beta-sheet protein.
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TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II.
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The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway.
  Mol Cell, 36, 255-266.  
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  Mol Cell, 36, 457-468.  
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PDB codes: 3fbi 3fbn
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19033456 C.D.Harvey, A.G.Ehrhardt, C.Cellurale, H.Zhong, R.Yasuda, R.J.Davis, and K.Svoboda (2008).
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Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together.
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16924229 A.Laine, and Z.Ronai (2007).
Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1.
  Oncogene, 26, 1477-1483.  
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Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1.
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PDB codes: 2jo9 2joc
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Homodimerization antagonizes nuclear export of survivin.
  Traffic, 8, 1495-1502.  
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An essential role for Pin1 in Xenopus laevis embryonic development revealed by specific inhibitors.
  Biol Chem, 388, 1103-1111.  
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The prolyl isomerase Pin1 affects Che-1 stability in response to apoptotic DNA damage.
  J Biol Chem, 282, 19685-19691.  
17892493 G.Lippens, I.Landrieu, and C.Smet (2007).
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
  FEBS J, 274, 5211-5222.  
17876319 K.P.Lu, G.Finn, T.H.Lee, and L.K.Nicholson (2007).
Prolyl cis-trans isomerization as a molecular timer.
  Nat Chem Biol, 3, 619-629.  
17878917 K.P.Lu, and X.Z.Zhou (2007).
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease.
  Nat Rev Mol Cell Biol, 8, 904-916.  
17706599 M.C.Herlevsen, and D.Theodorescu (2007).
Mass spectroscopic phosphoprotein mapping of Ral binding protein 1 (RalBP1/Rip1/RLIP76).
  Biochem Biophys Res Commun, 362, 56-62.  
17656366 M.D.Jennings, R.T.Blankley, M.Baron, A.P.Golovanov, and J.M.Avis (2007).
Specificity and autoregulation of Notch binding by tandem WW domains in suppressor of Deltex.
  J Biol Chem, 282, 29032-29042.
PDB code: 2jmf
17586778 M.Jäger, H.Nguyen, M.Dendle, M.Gruebele, and J.W.Kelly (2007).
Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and folding.
  Protein Sci, 16, 1495-1501.  
17766376 M.Jäger, M.Dendle, A.A.Fuller, and J.W.Kelly (2007).
A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function.
  Protein Sci, 16, 2306-2313.  
17686488 M.Meiyappan, G.Birrane, and J.A.Ladias (2007).
Structural basis for polyproline recognition by the FE65 WW domain.
  J Mol Biol, 372, 970-980.
PDB codes: 2ho2 2idh 2oei
17203101 P.E.Shaw (2007).
Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?
  EMBO Rep, 8, 40-45.  
17383430 R.Pang, T.K.Lee, R.T.Poon, S.T.Fan, K.B.Wong, Y.L.Kwong, and E.Tse (2007).
Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis.
  Gastroenterology, 132, 1088-1103.  
18025461 S.Ramón-Maiques, A.J.Kuo, D.Carney, A.G.Matthews, M.A.Oettinger, O.Gozani, and W.Yang (2007).
The plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2.
  Proc Natl Acad Sci U S A, 104, 18993-18998.
PDB codes: 2v83 2v85 2v86 2v87 2v88
17848966 S.Ruchaud, M.Carmena, and W.C.Earnshaw (2007).
Chromosomal passengers: conducting cell division.
  Nat Rev Mol Cell Biol, 8, 798-812.  
17164243 S.Ryser, T.Fujita, S.Tortola, I.Piuz, and W.Schlegel (2007).
The rate of c-fos transcription in vivo is continuously regulated at the level of elongation by dynamic stimulus-coupled recruitment of positive transcription elongation factor b.
  J Biol Chem, 282, 5075-5084.  
17612487 T.Dohi, F.Xia, and D.C.Altieri (2007).
Compartmentalized phosphorylation of IAP by protein kinase A regulates cytoprotection.
  Mol Cell, 27, 17-28.  
17334375 T.Peng, J.S.Zintsmaster, A.T.Namanja, and J.W.Peng (2007).
Sequence-specific dynamics modulate recognition specificity in WW domains.
  Nat Struct Mol Biol, 14, 325-331.  
17912258 T.R.Hupp, and M.Walkinshaw (2007).
Multienzyme assembly of a p53 transcription complex.
  Nat Struct Mol Biol, 14, 885-887.  
17766370 T.Sharpe, A.L.Jonsson, T.J.Rutherford, V.Daggett, and A.R.Fersht (2007).
The role of the turn in beta-hairpin formation during WW domain folding.
  Protein Sci, 16, 2233-2239.  
18006688 Y.X.Xu, and J.L.Manley (2007).
Pin1 modulates RNA polymerase II activity during the transcription cycle.
  Genes Dev, 21, 2950-2962.  
16253993 A.Gasch, S.Wiesner, P.Martin-Malpartida, X.Ramirez-Espain, L.Ruiz, and M.J.Macias (2006).
The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domains.
  J Biol Chem, 281, 356-364.
PDB code: 2b7e
16326109 A.J.Watson (2006).
An overview of apoptosis and the prevention of colorectal cancer.
  Crit Rev Oncol Hematol, 57, 107-121.  
16945100 D.A.Butterfield, H.M.Abdul, W.Opii, S.F.Newman, G.Joshi, M.A.Ansari, and R.Sultana (2006).
Pin1 in Alzheimer's disease.
  J Neurochem, 98, 1697-1706.  
16934447 D.C.Altieri (2006).
The case for survivin as a regulator of microtubule dynamics and cell-death decisions.
  Curr Opin Cell Biol, 18, 609-615.  
16759290 D.Du Pasquier, A.C.Phung, Q.Ymlahi-Ouazzani, L.Sinzelle, C.Ballagny, O.Bronchain, L.Du Pasquier, and A.Mazabraud (2006).
Survivin increased vascular development during Xenopus ontogenesis.
  Differentiation, 74, 244-253.  
16286474 E.Vojnic, B.Simon, B.D.Strahl, M.Sattler, and P.Cramer (2006).
Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription.
  J Biol Chem, 281, 13-15.
PDB code: 2c5z
16648162 F.Cecconi, C.Guardiani, and R.Livi (2006).
Testing simplified proteins models of the hPin1 WW domain.
  Biophys J, 91, 694-704.  
16522211 J.W.Mueller, D.Kessler, D.Neumann, T.Stratmann, P.Papatheodorou, C.Hartmann-Fatu, and P.Bayer (2006).
Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.
  BMC Mol Biol, 7, 9.  
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Targeting carcinogenesis: a role for the prolyl isomerase Pin1?
  Mol Carcinog, 45, 397-402.  
16644721 L.Yu, A.J.Mohamed, L.Vargas, A.Berglöf, G.Finn, K.P.Lu, and C.I.Smith (2006).
Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1.
  J Biol Chem, 281, 18201-18207.  
16807295 M.Jäger, Y.Zhang, J.Bieschke, H.Nguyen, M.Dendle, M.E.Bowman, J.P.Noel, M.Gruebele, and J.W.Kelly (2006).
Structure-function-folding relationship in a WW domain.
  Proc Natl Acad Sci U S A, 103, 10648-10653.
PDB codes: 1zcn 2f21
16274748 R.L.Neve, and D.L.McPhie (2006).
The cell cycle as a therapeutic target for Alzheimer's disease.
  Pharmacol Ther, 111, 99.  
16962308 S.M.Lens, G.Vader, and R.H.Medema (2006).
The case for Survivin as mitotic regulator.
  Curr Opin Cell Biol, 18, 616-622.  
16531238 V.Kanelis, M.C.Bruce, N.R.Skrynnikov, D.Rotin, and J.D.Forman-Kay (2006).
Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex.
  Structure, 14, 543-553.
PDB code: 2ez5
16302169 X.J.Wang, and F.A.Etzkorn (2006).
Peptidyl-prolyl isomerase inhibitors.
  Biopolymers, 84, 125-146.  
17065151 Y.Kato, T.Miyakawa, J.Kurita, and M.Tanokura (2006).
Structure of FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group II/III WW domains.
  J Biol Chem, 281, 40321-40329.
PDB code: 2dyf
15959902 A.C.Roque, and C.R.Lowe (2005).
Lessons from nature: On the molecular recognition elements of the phosphoprotein binding-domains.
  Biotechnol Bioeng, 91, 546-555.  
15576564 B.A.Joughin, B.Tidor, and M.B.Yaffe (2005).
A computational method for the analysis and prediction of protein:phosphopeptide-binding sites.
  Protein Sci, 14, 131-139.  
15702066 C.D.Lima (2005).
Inducing interactions with the CTD.
  Nat Struct Mol Biol, 12, 102-103.  
15665873 C.G.Noble, D.Hollingworth, S.R.Martin, V.Ennis-Adeniran, S.J.Smerdon, G.Kelly, I.A.Taylor, and A.Ramos (2005).
Key features of the interaction between Pcf11 CID and RNA polymerase II CTD.
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PDB code: 2bf0
15901493 D.L.Bentley (2005).
Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors.
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15867923 G.Wulf, G.Finn, F.Suizu, and K.P.Lu (2005).
Phosphorylation-specific prolyl isomerization: is there an underlying theme?
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15800888 J.F.Espinosa, F.A.Syud, and S.H.Gellman (2005).
An autonomously folding beta-hairpin derived from the human YAP65 WW domain: attempts to define a minimum ligand-binding motif.
  Biopolymers, 80, 303-311.  
15670305 J.P.Lee, K.H.Chang, J.H.Han, and H.S.Ryu (2005).
Survivin, a novel anti-apoptosis inhibitor, expression in uterine cervical cancer and relationship with prognostic factors.
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15894266 J.Plescia, W.Salz, F.Xia, M.Pennati, N.Zaffaroni, M.G.Daidone, M.Meli, T.Dohi, P.Fortugno, Y.Nefedova, D.I.Gabrilovich, G.Colombo, and D.C.Altieri (2005).
Rational design of shepherdin, a novel anticancer agent.
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15880548 L.J.Ball, R.Kühne, J.Schneider-Mergener, and H.Oschkinat (2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
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16314571 M.Li, H.P.Phatnani, Z.Guan, H.Sage, A.L.Greenleaf, and P.Zhou (2005).
Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.
  Proc Natl Acad Sci U S A, 102, 17636-17641.
PDB code: 2a7o
16176273 M.Minczuk, S.Mroczek, S.D.Pawlak, and P.P.Stepien (2005).
Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP.
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  16511241 N.Umadevi, S.Kumar, and N.Narayana (2005).
Crystallization and preliminary X-ray diffraction studies of the WW4 domain of the Nedd4-2 ubiquitin-protein ligase.
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16123044 P.Monje, J.Hernández-Losa, R.J.Lyons, M.D.Castellone, and J.S.Gutkind (2005).
Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1.
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16227615 P.Yi, R.C.Wu, J.Sandquist, J.Wong, S.Y.Tsai, M.J.Tsai, A.R.Means, and B.W.O'Malley (2005).
Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1).
  Mol Cell Biol, 25, 9687-9699.  
16055720 R.J.Ingham, K.Colwill, C.Howard, S.Dettwiler, C.S.Lim, J.Yu, K.Hersi, J.Raaijmakers, G.Gish, G.Mbamalu, L.Taylor, B.Yeung, G.Vassilovski, M.Amin, F.Chen, L.Matskova, G.Winberg, I.Ernberg, R.Linding, P.O'donnell, A.Starostine, W.Keller, P.Metalnikov, C.Stark, and T.Pawson (2005).
WW domains provide a platform for the assembly of multiprotein networks.
  Mol Cell Biol, 25, 7092-7106.  
16148005 S.Hausmann, H.Koiwa, S.Krishnamurthy, M.Hampsey, and S.Shuman (2005).
Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases.
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15728580 T.R.Gemmill, X.Wu, and S.D.Hanes (2005).
Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.
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16177795 W.P.Russ, D.M.Lowery, P.Mishra, M.B.Yaffe, and R.Ranganathan (2005).
Natural-like function in artificial WW domains.
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15171797 A.L.Albert, S.B.Lavoie, and M.Vincent (2004).
Multisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3.
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15241417 A.Meinhart, and P.Cramer (2004).
Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors.
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PDB codes: 1sz9 1sza
14695515 G.Lippens, J.M.Wieruszeski, A.Leroy, C.Smet, A.Sillen, L.Buée, and I.Landrieu (2004).
Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.
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14981252 J.Karanicolas, and C.L.Brooks (2004).
Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain.
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15189994 J.W.Stiller, and M.S.Cook (2004).
Functional unit of the RNA polymerase II C-terminal domain lies within heptapeptide pairs.
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  15111319 L.Bao, A.Kimzey, G.Sauter, J.M.Sowadski, K.P.Lu, and D.G.Wang (2004).
Prevalent overexpression of prolyl isomerase Pin1 in human cancers.
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15139812 M.B.Yaffe, and S.J.Smerdon (2004).
The use of in vitro peptide-library screens in the analysis of phosphoserine/threonine-binding domain structure and function.
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15485897 M.J.Smith, S.Kulkarni, and T.Pawson (2004).
FF domains of CA150 bind transcription and splicing factors through multiple weak interactions.
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15173166 O.Y.Fedoroff, S.A.Townson, A.P.Golovanov, M.Baron, and J.M.Avis (2004).
The structure and dynamics of tandem WW domains in a negative regulator of notch signaling, Suppressor of deltex.
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PDB code: 1tk7
14681225 R.Ley, K.E.Ewings, K.Hadfield, E.Howes, K.Balmanno, and S.J.Cook (2004).
Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover.
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15114340 S.Hahn (2004).
Structure and mechanism of the RNA polymerase II transcription machinery.
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14981505 T.Kuzuhara, and M.Horikoshi (2004).
A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing.
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15133021 Y.Kato, K.Nagata, M.Takahashi, L.Lian, J.J.Herrero, M.Sudol, and M.Tanokura (2004).
Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.
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14532005 A.E.Elia, P.Rellos, L.F.Haire, J.W.Chao, F.J.Ivins, K.Hoepker, D.Mohammad, L.C.Cantley, S.J.Smerdon, and M.B.Yaffe (2003).
The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain.
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PDB code: 1umw
12906819 A.Greenleaf (2003).
Getting a grip on the CTD of Pol II.
  Structure, 11, 900-902.  
12820968 C.Fabrega, V.Shen, S.Shuman, and C.D.Lima (2003).
Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II.
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PDB code: 1p16
12686540 D.M.Jacobs, K.Saxena, M.Vogtherr, P.Bernado, M.Pons, and K.M.Fiebig (2003).
Peptide binding induces large scale changes in inter-domain mobility in human Pin1.
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12721297 E.Bayer, S.Goettsch, J.W.Mueller, B.Griewel, E.Guiberman, L.M.Mayr, and P.Bayer (2003).
Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding.
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PDB codes: 1nmv 1nmw
12809608 G.G.Simpson, P.P.Dijkwel, V.Quesada, I.Henderson, and C.Dean (2003).
FY is an RNA 3' end-processing factor that interacts with FCA to control the Arabidopsis floral transition.
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14592974 K.Y.Cheng, E.D.Lowe, J.Sinclair, E.A.Nigg, and L.N.Johnson (2003).
The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex.
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PDB codes: 1q4k 1q4o
12592019 L.Otte, U.Wiedemann, B.Schlegel, J.R.Pires, M.Beyermann, P.Schmieder, G.Krause, R.Volkmer-Engert, J.Schneider-Mergener, and H.Oschkinat (2003).
WW domain sequence activity relationships identified using ligand recognition propensities of 42 WW domains.
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12897238 N.Ferguson, J.Berriman, M.Petrovich, T.D.Sharpe, J.T.Finch, and A.R.Fersht (2003).
Rapid amyloid fiber formation from the fast-folding WW domain FBP28.
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12654927 P.C.Henry, V.Kanelis, M.C.O'Brien, B.Kim, I.Gautschi, J.Forman-Kay, L.Schild, and D.Rotin (2003).
Affinity and specificity of interactions between Nedd4 isoforms and the epithelial Na+ channel.
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12757758 P.E.Shaw, and J.Saxton (2003).
Ternary complex factors: prime nuclear targets for mitogen-activated protein kinases.
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12942140 S.Buratowski (2003).
The CTD code.
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12553912 S.Orlicky, X.Tang, A.Willems, M.Tyers, and F.Sicheri (2003).
Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
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PDB code: 1nex
12702867 T.Pawson, and P.Nash (2003).
Assembly of cell regulatory systems through protein interaction domains.
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12573694 T.Uchida, M.Takamiya, M.Takahashi, H.Miyashita, H.Ikeda, T.Terada, Y.Matsuo, M.Shirouzu, S.Yokoyama, F.Fujimori, and T.Hunter (2003).
Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation.
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12471608 T.Wang, and R.C.Wade (2003).
Implicit solvent models for flexible protein-protein docking by molecular dynamics simulation.
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14600023 Y.X.Xu, Y.Hirose, X.Z.Zhou, K.P.Lu, and J.L.Manley (2003).
Pin1 modulates the structure and function of human RNA polymerase II.
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12150824 D.S.O'Connor, N.R.Wall, A.C.Porter, and D.C.Altieri (2002).
A p34(cdc2) survival checkpoint in cancer.
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  11805043 G.Devasahayam, V.Chaturvedi, and S.D.Hanes (2002).
The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans.
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11786999 J.A.Kowalski, K.Liu, and J.W.Kelly (2002).
NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.
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PDB code: 2kcf
11978535 K.P.Lu, Y.C.Liou, and X.Z.Zhou (2002).
Pinning down proline-directed phosphorylation signaling.
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12052773 P.E.Shaw (2002).
Peptidyl-prolyl isomerases: a new twist to transcription.
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12397362 P.Zacchi, M.Gostissa, T.Uchida, C.Salvagno, F.Avolio, S.Volinia, Z.Ronai, G.Blandino, C.Schneider, and G.Del Sal (2002).
The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults.
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11805292 Y.C.Liou, A.Ryo, H.K.Huang, P.J.Lu, R.Bronson, F.Fujimori, T.Uchida, T.Hunter, and K.P.Lu (2002).
Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes.
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11751914 Y.Kato, M.Ito, K.Kawai, K.Nagata, and M.Tanokura (2002).
Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building.
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12032548 Y.Kato, S.Misra, R.Puertollano, J.H.Hurley, and J.S.Bonifacino (2002).
Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.
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PDB code: 1lf8
12401491 Z.Huang (2002).
The chemical biology of apoptosis. Exploring protein-protein interactions and the life and death of cells with small molecules.
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11604498 A.C.Goldstrohm, T.R.Albrecht, C.Suñé, M.T.Bedford, and M.A.Garcia-Blanco (2001).
The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1.
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11551507 C.L.Kielkopf, N.A.Rodionova, M.R.Green, and S.K.Burley (2001).
A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.
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PDB code: 1jmt
11733216 D.C.Altieri (2001).
The molecular basis and potential role of survivin in cancer diagnosis and therapy.
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11241639 F.Toepert, J.R.Pires, C.Landgraf, H.Oschkinat, and J.Schneider-Mergener (2001).
Synthesis of an Array Comprising 837 Variants of the hYAP WW Protein Domain This work was supported by the DFG (INK 16/B1-1), by the Fonds der Chemischen Industrie, and by the Universitätsklinikum Charité Berlin.
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11331761 J.C.Lougheed, J.M.Holton, T.Alber, J.F.Bazan, and T.M.Handel (2001).
Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins.
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PDB code: 1i1j
11179890 J.H.Laity, B.M.Lee, and P.E.Wright (2001).
Zinc finger proteins: new insights into structural and functional diversity.
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11306348 J.Kasanov, G.Pirozzi, A.J.Uveges, and B.K.Kay (2001).
Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities.
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11511363 J.W.Wu, A.E.Cocina, J.Chai, B.A.Hay, and Y.Shi (2001).
Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.
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PDB codes: 1jd4 1jd5 1jd6
11248545 M.B.Yaffe, and A.E.Elia (2001).
Phosphoserine/threonine-binding domains.
  Curr Opin Cell Biol, 13, 131-138.  
11257232 S.J.Riedl, M.Renatus, R.Schwarzenbacher, Q.Zhou, C.Sun, S.W.Fesik, R.C.Liddington, and G.S.Salvesen (2001).
Structural basis for the inhibition of caspase-3 by XIAP.
  Cell, 104, 791-800.
PDB code: 1i3o
11420447 X.Jiang, J.Kowalski, and J.W.Kelly (2001).
Increasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain.
  Protein Sci, 10, 1454-1465.  
  11257231 Y.Huang, Y.C.Park, R.L.Rich, D.Segal, D.G.Myszka, and H.Wu (2001).
Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain.
  Cell, 104, 781-790.
PDB code: 1i4o
11007472 J.C.Reed, and J.R.Bischoff (2000).
BIRinging chromosomes through cell division--and survivin' the experience.
  Cell, 102, 545-548.  
11206058 P.A.Dalby, R.H.Hoess, and W.F.DeGrado (2000).
Evolution of binding affinity in a WW domain probed by phage display.
  Protein Sci, 9, 2366-2376.  
11057900 S.W.Fesik (2000).
Insights into programmed cell death through structural biology.
  Cell, 103, 273-282.  
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 codes are shown on the right.