PDBsum entry 1jst

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protein ligands metals Protein-protein interface(s) links
Complex (protein kinase/cyclin) PDB id
Protein chains
298 a.a. *
258 a.a. *
ATP ×2
_MN ×2
Waters ×98
* Residue conservation analysis
PDB id:
Name: Complex (protein kinase/cyclin)
Title: Phosphorylated cyclin-dependent kinase-2 bound to cyclin a
Structure: Cyclin-dependent kinase-2. Chain: a, c. Synonym: cdk2. Engineered: yes. Other_details: phosphorylated. Cyclin a. Chain: b, d. Fragment: residues 173-432. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: sf9. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Other_details: cyclin a-bound form phosphorylated on thr 16 vitro using a cdk-activating kinase consisting of the cycli complex.
Biol. unit: Tetramer (from PQS)
2.60Å     R-factor:   0.200    
Authors: A.A.Russo,P.D.Jeffrey,N.P.Pavletich
Key ref: A.A.Russo et al. (1996). Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol, 3, 696-700. PubMed id: 8756328
03-Jul-96     Release date:   11-Jan-97    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2
298 a.a.
298 a.a.*
Protein chains
Pfam   ArchSchema ?
P20248  (CCNA2_HUMAN) -  Cyclin-A2
432 a.a.
258 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.  - Cyclin-dependent kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
Bound ligand (Het Group name = ATP)
corresponds exactly
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cyclin-dependent protein kinase holoenzyme complex   15 terms 
  Biological process     regulation of gene silencing   30 terms 
  Biochemical function     nucleotide binding     13 terms  


Nat Struct Biol 3:696-700 (1996)
PubMed id: 8756328  
Structural basis of cyclin-dependent kinase activation by phosphorylation.
A.A.Russo, P.D.Jeffrey, N.P.Pavletich.
Cyclin-dependent kinase (CDK)-cyclin complexes require phosphorylation on the CDK subunit for full activation of their Ser/Thr protein kinase activity. The crystal structure of the phosphorylated CDK2-CyclinA-ATP gamma S complex has been determined at 2.6 A resolution. The phosphate group, which is on the regulatory T-loop of CDK2, is mostly buried, its charge being neutralized by three Arg side chains. The arginines help extend the influence of the phosphate group through a network of hydrogen bonds to both CDK2 and cyclinA. Comparison with the unphosphorylated CDK2-CyclinA complex shows that the T-loop moves by as much as 7 A, and this affects the putative substrate binding site as well as resulting in additional CDK2-CyclinA contacts. The phosphate group thus acts as a major organizing centre in the CDK2-CyclinA complex.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23064647 S.Hughes, F.Elustondo, A.Di Fonzo, F.G.Leroux, A.C.Wong, A.P.Snijders, S.J.Matthews, and P.Cherepanov (2012).
Crystal structure of human CDC7 kinase in complex with its activator DBF4.
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PDB codes: 4f99 4f9a 4f9b 4f9c
21205204 G.Ghosh, and J.A.Adams (2011).
Phosphorylation mechanism and structure of serine-arginine protein kinases.
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20836132 J.Węsierska-Gądek, M.Maurer, N.Zulehner, and O.Komina (2011).
Whether to target single or multiple CDKs for therapy? That is the question.
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20013135 B.Zhang, Z.C.Su, T.E.Tay, and V.B.Tan (2010).
Mechanism of CDK5 activation revealed by steered molecular dynamics simulations and energy calculations.
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Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates.
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PDB code: 3iec
20432069 J.H.Bae, and J.Schlessinger (2010).
Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases.
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Putting one step before the other: distinct activation pathways for Cdk1 and Cdk2 bring order to the mammalian cell cycle.
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Cell-cycle markers and biosensors.
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20347419 R.W.Deibler, and M.W.Kirschner (2010).
Quantitative reconstitution of mitotic CDK1 activation in somatic cell extracts.
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21044075 S.Hisanaga, and R.Endo (2010).
Regulation and role of cyclin-dependent kinase activity in neuronal survival and death.
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21134645 T.N.Lombana, N.Echols, M.C.Good, N.D.Thomsen, H.L.Ng, A.E.Greenstein, A.M.Falick, D.S.King, and T.Alber (2010).
Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB.
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PDB code: 3orm
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Computational studies of protein regulation by post-translational phosphorylation.
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19075005 A.Ray, M.K.James, S.Larochelle, R.P.Fisher, and S.W.Blain (2009).
p27Kip1 inhibits cyclin D-cyclin-dependent kinase 4 by two independent modes.
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Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization.
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PDB code: 2wb8
19101503 G.S.Baldwin (2009).
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Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.
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18971272 M.Zhou, K.Huang, K.J.Jung, W.K.Cho, Z.Klase, F.Kashanchi, C.A.Pise-Masison, and J.N.Brady (2009).
Bromodomain protein Brd4 regulates human immunodeficiency virus transcription through phosphorylation of CDK9 at threonine 29.
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19237565 P.J.Day, A.Cleasby, I.J.Tickle, M.O'Reilly, J.E.Coyle, F.P.Holding, R.L.McMenamin, J.Yon, R.Chopra, C.Lengauer, and H.Jhoti (2009).
Crystal structure of human CDK4 in complex with a D-type cyclin.
  Proc Natl Acad Sci U S A, 106, 4166-4170.
PDB codes: 2w96 2w99 2w9f 2w9z
  19498957 P.Towb, H.Sun, and S.A.Wasserman (2009).
Tube Is an IRAK-4 homolog in a Toll pathway adapted for development and immunity.
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Characterization of Cdk9 T-loop phosphorylation in resting and activated CD4(+) T lymphocytes.
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19387490 S.Cho, S.Schroeder, K.Kaehlcke, H.S.Kwon, A.Pedal, E.Herker, M.Schnoelzer, and M.Ott (2009).
Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells.
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19680222 S.Vigneron, E.Brioudes, A.Burgess, J.C.Labbé, T.Lorca, and A.Castro (2009).
Greatwall maintains mitosis through regulation of PP2A.
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19237555 T.Takaki, A.Echalier, N.R.Brown, T.Hunt, J.A.Endicott, and M.E.Noble (2009).
The structure of CDK4/cyclin D3 has implications for models of CDK activation.
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PDB code: 3g33
17873913 C.Denicourt, P.Legault, F.A.McNabb, and E.Rassart (2008).
Human and mouse cyclin D2 splice variants: transforming activity and subcellular localization.
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18042686 I.Bártová, J.Koca, and M.Otyepka (2008).
Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation.
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18470542 I.Bártová, J.Koca, and M.Otyepka (2008).
Regulatory phosphorylation of cyclin-dependent kinase 2: insights from molecular dynamics simulations.
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19061641 K.A.Merrick, S.Larochelle, C.Zhang, J.J.Allen, K.M.Shokat, and R.P.Fisher (2008).
Distinct activation pathways confer cyclin-binding specificity on Cdk1 and Cdk2 in human cells.
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17908796 M.K.James, A.Ray, D.Leznova, and S.W.Blain (2008).
Differential modification of p27Kip1 controls its cyclin D-cdk4 inhibitory activity.
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18483222 R.Chen, M.Liu, H.Li, Y.Xue, W.N.Ramey, N.He, N.Ai, H.Luo, Y.Zhu, N.Zhou, and Q.Zhou (2008).
PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling.
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18566585 S.Baumli, G.Lolli, E.D.Lowe, S.Troiani, L.Rusconi, A.N.Bullock, J.E.Debreczeni, S.Knapp, and L.N.Johnson (2008).
The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation.
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PDB codes: 2ivx 3blh 3blq 3blr
17937404 T.O.Fischmann, A.Hruza, J.S.Duca, L.Ramanathan, T.Mayhood, W.T.Windsor, H.V.Le, T.J.Guzi, M.P.Dwyer, K.Paruch, R.J.Doll, E.Lees, D.Parry, W.Seghezzi, and V.Madison (2008).
Structure-guided discovery of cyclin-dependent kinase inhibitors.
  Biopolymers, 89, 372-379.
PDB codes: 2r3f 2r3g 2r3h 2r3i 2r3j 2r3k 2r3l 2r3m 2r3n 2r3o 2r3p 2r3q 2r3r
18491300 W.Selleck, and S.Tan (2008).
Recombinant protein complex expression in E. coli.
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17299750 I.Kufareva, L.Budagyan, E.Raush, M.Totrov, and R.Abagyan (2007).
PIER: protein interface recognition for structural proteomics.
  Proteins, 67, 400-417.  
17912359 J.D.Knight, B.Qian, D.Baker, and R.Kothary (2007).
Conservation, variability and the modeling of active protein kinases.
  PLoS ONE, 2, e982.  
17286863 J.Gu, and P.E.Bourne (2007).
Identifying allosteric fluctuation transitions between different protein conformational states as applied to Cyclin Dependent Kinase 2.
  BMC Bioinformatics, 8, 45.  
17095507 J.P.Welburn, J.A.Tucker, T.Johnson, L.Lindert, M.Morgan, A.Willis, M.E.Noble, and J.A.Endicott (2007).
How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A.
  J Biol Chem, 282, 3173-3181.
PDB code: 2cjm
17169370 K.Baek, R.S.Brown, G.Birrane, and J.A.Ladias (2007).
Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9.
  J Mol Biol, 366, 563-573.
PDB code: 2i53
18042456 K.Huang, I.Ferrin-O'Connell, W.Zhang, G.A.Leonard, E.K.O'Shea, and F.A.Quiocho (2007).
Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway.
  Mol Cell, 28, 614-623.
PDB codes: 2pk9 2pmi
17386261 S.Larochelle, K.A.Merrick, M.E.Terret, L.Wohlbold, N.M.Barboza, C.Zhang, K.M.Shokat, P.V.Jallepalli, and R.P.Fisher (2007).
Requirements for Cdk7 in the assembly of Cdk1/cyclin B and activation of Cdk2 revealed by chemical genetics in human cells.
  Mol Cell, 25, 839-850.  
17914234 V.S.Gowri, K.Anamika, S.Gore, and N.Srinivasan (2007).
Analysis on sliding helices and strands in protein structural comparisons: a case study with protein kinases.
  J Biosci, 32, 921-928.  
17063377 W.S.Chao, M.D.Serpe, Y.Jia, W.L.Shelver, J.V.Anderson, and M.Umeda (2007).
Potential roles for autophosphorylation, kinase activity, and abundance of a CDK-activating kinase (Ee;CDKF;1) during growth in leafy spurge.
  Plant Mol Biol, 63, 365-379.  
16488127 A.R.Nebreda (2006).
CDK activation by non-cyclin proteins.
  Curr Opin Cell Biol, 18, 192-198.  
17054019 B.Zhang, V.B.Tan, K.M.Lim, and T.E.Tay (2006).
Molecular dynamics simulations on the inhibition of cyclin-dependent kinases 2 and 5 in the presence of activators.
  J Comput Aided Mol Des, 20, 395-404.  
16628247 E.S.Groban, A.Narayanan, and M.P.Jacobson (2006).
Conformational changes in protein loops and helices induced by post-translational phosphorylation.
  PLoS Comput Biol, 2, e32.  
16935860 I.Bertani, L.Rusconi, F.Bolognese, G.Forlani, B.Conca, L.De Monte, G.Badaracco, N.Landsberger, and C.Kilstrup-Nielsen (2006).
Functional consequences of mutations in CDKL5, an X-linked gene involved in infantile spasms and mental retardation.
  J Biol Chem, 281, 32048-32056.  
16584130 J.Sridhar, N.Akula, and N.Pattabiraman (2006).
Selectivity and potency of cyclin-dependent kinase inhibitors.
  AAPS J, 8, E204-E221.  
16809767 J.Yue, and J.E.Ferrell (2006).
Mechanistic studies of the mitotic activation of Mos.
  Mol Cell Biol, 26, 5300-5309.  
16292742 M.De Vivo, A.Cavalli, G.Bottegoni, P.Carloni, and M.Recanatini (2006).
Role of phosphorylated Thr160 for the activation of the CDK2/Cyclin A complex.
  Proteins, 62, 89-98.  
16407256 M.Otyepka, I.Bártová, Z.Kríz, and J.Koca (2006).
Different mechanisms of CDK5 and CDK2 activation as revealed by CDK5/p25 and CDK2/cyclin A dynamics.
  J Biol Chem, 281, 7271-7281.  
17001081 N.Canela, M.Orzáez, R.Fucho, F.Mateo, R.Gutierrez, A.Pineda-Lucena, O.Bachs, and E.Pérez-Payá (2006).
Identification of an hexapeptide that binds to a surface pocket in cyclin A and inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A.
  J Biol Chem, 281, 35942-35953.  
16959964 Q.Zhou, and J.H.Yik (2006).
The Yin and Yang of P-TEFb regulation: implications for human immunodeficiency virus gene expression and global control of cell growth and differentiation.
  Microbiol Mol Biol Rev, 70, 646-659.  
16917500 R.Jauch, M.K.Cho, S.Jäkel, C.Netter, K.Schreiter, B.Aicher, M.Zweckstetter, H.Jäckle, and M.C.Wahl (2006).
Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment.
  EMBO J, 25, 4020-4032.
PDB codes: 2hw6 2hw7
16327805 S.Larochelle, J.Batliner, M.J.Gamble, N.M.Barboza, B.C.Kraybill, J.D.Blethrow, K.M.Shokat, and R.P.Fisher (2006).
Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics.
  Nat Struct Mol Biol, 13, 55-62.  
15687503 A.Z.Ansari, A.Ogirala, and M.Ptashne (2005).
Transcriptional activating regions target attached substrates to a cyclin-dependent kinase.
  Proc Natl Acad Sci U S A, 102, 2346-2349.  
15515182 Anamika, N.Srinivasan, and A.Krupa (2005).
A genomic perspective of protein kinases in Plasmodium falciparum.
  Proteins, 58, 180-189.  
15649889 C.Gondeau, S.Gerbal-Chaloin, P.Bello, G.Aldrian-Herrada, M.C.Morris, and G.Divita (2005).
Design of a novel class of peptide inhibitors of cyclin-dependent kinase/cyclin activation.
  J Biol Chem, 280, 13793-13800.  
15695825 C.P.Barrett, and M.E.Noble (2005).
Molecular motions of human cyclin-dependent kinase 2.
  J Biol Chem, 280, 13993-14005.  
15741170 D.Komander, G.Kular, M.Deak, D.R.Alessi, and D.M.van Aalten (2005).
Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding.
  J Biol Chem, 280, 18797-18802.
PDB code: 2biy
15618230 G.H.Iyer, M.J.Moore, and S.S.Taylor (2005).
Consequences of lysine 72 mutation on the phosphorylation and activation state of cAMP-dependent kinase.
  J Biol Chem, 280, 8800-8807.  
15647260 G.Zhu, K.Fujii, N.Belkina, Y.Liu, M.James, J.Herrero, and S.Shaw (2005).
Exceptional disfavor for proline at the P + 1 position among AGC and CAMK kinases establishes reciprocal specificity between them and the proline-directed kinases.
  J Biol Chem, 280, 10743-10748.  
15798205 J.H.Kim, J.H.Kim, M.Ohba, P.G.Suh, and S.H.Ryu (2005).
Novel functions of the phospholipase D2-Phox homology domain in protein kinase Czeta activation.
  Mol Cell Biol, 25, 3194-3208.  
15671017 M.Chinami, Y.Yano, X.Yang, S.Salahuddin, K.Moriyama, M.Shiroishi, H.Turner, T.Shirakawa, and C.N.Adra (2005).
Binding of HTm4 to cyclin-dependent kinase (Cdk)-associated phosphatase (KAP).Cdk2.cyclin A complex enhances the phosphatase activity of KAP, dissociates cyclin A, and facilitates KAP dephosphorylation of Cdk2.
  J Biol Chem, 280, 17235-17242.  
15893667 M.Lei, M.A.Robinson, and S.C.Harrison (2005).
The active conformation of the PAK1 kinase domain.
  Structure, 13, 769-778.
PDB codes: 1yhv 1yhw
15664993 P.Kaldis (2005).
The N-terminal peptide of the Kaposi's sarcoma-associated herpesvirus (KSHV)-cyclin determines substrate specificity.
  J Biol Chem, 280, 11165-11174.  
15660127 R.Honda, E.D.Lowe, E.Dubinina, V.Skamnaki, A.Cook, N.R.Brown, and L.N.Johnson (2005).
The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles.
  EMBO J, 24, 452-463.
PDB code: 1w98
15939018 S.W.Cowan-Jacob, G.Fendrich, P.W.Manley, W.Jahnke, D.Fabbro, J.Liebetanz, and T.Meyer (2005).
The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation.
  Structure, 13, 861-871.
PDB code: 1y57
15037601 C.Preisinger, B.Short, V.De Corte, E.Bruyneel, A.Haas, R.Kopajtich, J.Gettemans, and F.A.Barr (2004).
YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta.
  J Cell Biol, 164, 1009-1020.  
15096628 F.F.Miranda, M.Thórólfsson, K.Teigen, J.M.Sanchez-Ruiz, and A.Martínez (2004).
Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylase.
  Protein Sci, 13, 1219-1226.  
15133164 I.Bártová, M.Otyepka, Z.Kríz, and J.Koca (2004).
Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation; a molecular dynamics study reveals the functional importance of the glycine-rich loop.
  Protein Sci, 13, 1449-1457.  
15499549 J.Tao, H.Van Esch, M.Hagedorn-Greiwe, K.Hoffmann, B.Moser, M.Raynaud, J.Sperner, J.P.Fryns, E.Schwinger, J.Gécz, H.H.Ropers, and V.M.Kalscheuer (2004).
Mutations in the X-linked cyclin-dependent kinase-like 5 (CDKL5/STK9) gene are associated with severe neurodevelopmental retardation.
  Am J Hum Genet, 75, 1149-1154.  
15292186 L.Jin, S.Pluskey, E.C.Petrella, S.M.Cantin, J.C.Gorga, M.J.Rynkiewicz, P.Pandey, J.E.Strickler, R.E.Babine, D.T.Weaver, and K.J.Seidl (2004).
The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors.
  J Biol Chem, 279, 42818-42825.
PDB code: 1u59
15343278 N.J.Dibb, S.M.Dilworth, and C.D.Mol (2004).
Switching on kinases: oncogenic activation of BRAF and the PDGFR family.
  Nat Rev Cancer, 4, 718-727.  
15273306 N.Kannan, and A.F.Neuwald (2004).
Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha.
  Protein Sci, 13, 2059-2077.  
14701845 Q.Zhao, F.Boschelli, A.J.Caplan, and K.T.Arndt (2004).
Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4.
  J Biol Chem, 279, 12560-12564.  
14627702 R.Chen, Z.Yang, and Q.Zhou (2004).
Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA.
  J Biol Chem, 279, 4153-4160.  
12869192 E.De Moliner, N.R.Brown, and L.N.Johnson (2003).
Alternative binding modes of an inhibitor to two different kinases.
  Eur J Biochem, 270, 3174-3181.
PDB code: 1p5e
12688339 G.P.Studzinski, and J.S.Harrison (2003).
The neuronal cyclin-dependent kinase 5 activator p35Nck5a and Cdk5 activity in monocytic cells.
  Leuk Lymphoma, 44, 235-240.  
12972617 M.C.Keogh, V.Podolny, and S.Buratowski (2003).
Bur1 kinase is required for efficient transcription elongation by RNA polymerase II.
  Mol Cell Biol, 23, 7005-7018.  
12499371 M.J.Moore, J.A.Adams, and S.S.Taylor (2003).
Structural basis for peptide binding in protein kinase A. Role of glutamic acid 203 and tyrosine 204 in the peptide-positioning loop.
  J Biol Chem, 278, 10613-10618.  
12556199 N.C.Waters, and J.A.Geyer (2003).
Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development.
  Expert Opin Ther Targets, 7, 7.  
12789688 T.Honma (2003).
Recent advances in de novo design strategy for practical lead identification.
  Med Res Rev, 23, 606-632.  
12904290 Y.Pei, and S.Shuman (2003).
Characterization of the Schizosaccharomyces pombe Cdk9/Pch1 protein kinase: Spt5 phosphorylation, autophosphorylation, and mutational analysis.
  J Biol Chem, 278, 43346-43356.  
12359726 A.A.Kitazono, and S.J.Kron (2002).
An essential function of yeast cyclin-dependent kinase Cdc28 maintains chromosome stability.
  J Biol Chem, 277, 48627-48634.  
12044161 A.Cook, E.D.Lowe, E.D.Chrysina, V.T.Skamnaki, N.G.Oikonomakos, and L.N.Johnson (2002).
Structural studies on phospho-CDK2/cyclin A bound to nitrate, a transition state analogue: implications for the protein kinase mechanism.
  Biochemistry, 41, 7301-7311.
PDB code: 1gy3
12146964 B.E.Aubol, B.Nolen, D.Vu, G.Ghosh, and J.A.Adams (2002).
Mechanistic insights into Sky1p, a yeast homologue of the mammalian SR protein kinases.
  Biochemistry, 41, 10002-10009.  
12361946 C.M.Stultz, A.D.Levin, and E.R.Edelman (2002).
Phosphorylation-induced conformational changes in a mitogen-activated protein kinase substrate. Implications for tyrosine hydroxylase activation.
  J Biol Chem, 277, 47653-47661.  
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Crystal structure of aurora-2, an oncogenic serine/threonine kinase.
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PDB code: 1muo
11807175 I.R.Hardcastle, B.T.Golding, and R.J.Griffin (2002).
Designing inhibitors of cyclin-dependent kinases.
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11891112 K.E.Prehoda, and W.A.Lim (2002).
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12081504 L.M.Stevenson, M.S.Deal, J.C.Hagopian, and J.Lew (2002).
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12191604 L.N.Johnson, E.De Moliner, N.R.Brown, H.Song, D.Barford, J.A.Endicott, and M.E.Noble (2002).
Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2.
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11839796 M.C.Keogh, E.J.Cho, V.Podolny, and S.Buratowski (2002).
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12015977 M.Huse, and J.Kuriyan (2002).
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12359725 N.H.Lents, S.M.Keenan, C.Bellone, and J.J.Baldassare (2002).
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12244298 T.G.Davies, J.Bentley, C.E.Arris, F.T.Boyle, N.J.Curtin, J.A.Endicott, A.E.Gibson, B.T.Golding, R.J.Griffin, I.R.Hardcastle, P.Jewsbury, L.N.Johnson, V.Mesguiche, D.R.Newell, M.E.Noble, J.A.Tucker, L.Wang, and H.J.Whitfield (2002).
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PDB codes: 1h1p 1h1q 1h1r 1h1s
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PDB code: 1jow
11583627 C.Tarricone, R.Dhavan, J.Peng, L.B.Areces, L.H.Tsai, and A.Musacchio (2001).
Structure and regulation of the CDK5-p25(nck5a) complex.
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PDB code: 1h4l
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Checkpoint genes in cancer.
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11463386 H.Song, N.Hanlon, N.R.Brown, M.E.Noble, L.N.Johnson, and D.Barford (2001).
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PDB codes: 1fpz 1fq1
11495789 H.Stals, and D.Inzé (2001).
When plant cells decide to divide.
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11532001 J.K.Holmes, and M.J.Solomon (2001).
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11732181 P.C.John, M.Mews, and R.Moore (2001).
Cyclin/Cdk complexes: their involvement in cell cycle progression and mitotic division.
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11248668 R.B.Maccioni, C.Otth, I.I.Concha, and J.P.Muñoz (2001).
The protein kinase Cdk5. Structural aspects, roles in neurogenesis and involvement in Alzheimer's pathology.
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11440715 R.Dajani, E.Fraser, S.M.Roe, N.Young, V.Good, T.C.Dale, and L.H.Pearl (2001).
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PDB codes: 1fvt 1fvv
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The 1.7 A crystal structure of human cell cycle checkpoint kinase Chk1: implications for Chk1 regulation.
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Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors.
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Protein-protein interactions in receptor activation and intracellular signalling.
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Mechanism of biological synergy between cellular Src and epidermal growth factor receptor.
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Cyclin-dependent kinases: inhibition and substrate recognition.
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Activating phosphorylation of the Kin28p subunit of yeast TFIIH by Cak1p.
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Directed evolution to bypass cyclin requirements for the Cdc28p cyclin-dependent kinase.
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The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts.
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Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase.
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PDB code: 1bx6
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PDB codes: 1b38 1b39
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Regulation of cyclin-dependent kinase 5 catalytic activity by phosphorylation.
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Identification of substrate binding site of cyclin-dependent kinase 5.
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PDB code: 1cm8
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Autophosphorylation dependent destabilization of the insulin receptor kinase domain: tryptophan-1175 reports changes in the catalytic cleft.
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Catalytic mechanism of phosphorylase kinase probed by mutational studies.
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PDB code: 1ql6
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Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
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PDB code: 2src
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Effects of p21(Cip1/Waf1) at both the G1/S and the G2/M cell cycle transitions: pRb is a critical determinant in blocking DNA replication and in preventing endoreduplication.
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Mitotic phosphorylation of Bcl-2 during normal cell cycle progression and Taxol-induced growth arrest.
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Indole-3-carbinol inhibits the expression of cyclin-dependent kinase-6 and induces a G1 cell cycle arrest of human breast cancer cells independent of estrogen receptor signaling.
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Fission yeast Csk1 is a CAK-activating kinase (CAKAK).
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The RNA polymerase II general transcription factors: past, present, and future.
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Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.
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Human general transcription factor TFIIB: conformational variability and interaction with VP16 activation domain.
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PDB code: 1tfb
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Molecular evolution allows bypass of the requirement for activation loop phosphorylation of the Cdc28 cyclin-dependent kinase.
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Glucocorticoids stimulate p21 gene expression by targeting multiple transcriptional elements within a steroid responsive region of the p21waf1/cip1 promoter in rat hepatoma cells.
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Structural principles in cell-cycle control: beyond the CDKs.
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Isolation and characterization of new alleles of the cyclin-dependent kinase gene CDC28 with cyclin-specific functional and biochemical defects.
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The therapeutic potential of targeting the cell cycle.
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Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.
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The plant cell cycle in context.
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A rice homolog of Cdk7/MO15 phosphorylates both cyclin-dependent protein kinases and the carboxy-terminal domain of RNA polymerase II.
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Mutations in the activation loop tyrosine of the oncoprotein v-Fps.
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Site-specific phosphorylation of Lys-Ser-Pro repeat peptides from neurofilament H by cyclin-dependent kinase 5: structural basis for substrate recognition.
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The molecular mechanism of mitotic inhibition of TFIIH is mediated by phosphorylation of CDK7.
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Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.
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Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase.
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Recent advances on cyclins, CDKs and CDK inhibitors.
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Cyclin-dependent kinases: engines, clocks, and microprocessors.
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The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.
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Interactions of cyclins with cyclin-dependent kinases: a common interactive mechanism.
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A dominant-negative cyclin D1 mutant prevents nuclear import of cyclin-dependent kinase 4 (CDK4) and its phosphorylation by CDK-activating kinase.
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Partial activation of muscle phosphorylase by replacement of serine 14 with acidic residues at the site of regulatory phosphorylation.
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Cyclin-dependent kinase inhibitors: the age of crystals.
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The cell cycle and cancer.
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Distinct phosphorylation signals converge at the catalytic center in glycogen phosphorylases.
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Regulation of CDK7 substrate specificity by MAT1 and TFIIH.
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The cyclin box fold: protein recognition in cell-cycle and transcription control.
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CDKs and cyclins in transition(s).
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Identification of functional domains in the neuronal Cdk5 activator protein.
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Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog.
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PDB code: 1ir3
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Differential interaction of the cyclin-dependent kinase (Cdk) inhibitor p27Kip1 with cyclin A-Cdk2 and cyclin D2-Cdk4.
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The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.
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The dynamics of cyclin dependent kinase structure.
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Control by phosphorylation.
  Curr Opin Struct Biol, 6, 762-769.  
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