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PDBsum entry 1buh

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protein Protein-protein interface(s) links
Transferase PDB id
1buh
Jmol
Contents
Protein chains
287 a.a. *
70 a.a. *
Waters ×127
* Residue conservation analysis
PDB id:
1buh
Name: Transferase
Title: Crystal structure of the human cdk2 kinase complex with cell cycle-regulatory protein ckshs1
Structure: Protein (cdk2 human). Chain: a. Engineered: yes. Protein (ckshs1 human). Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.190     R-free:   0.250
Authors: Y.Bourne,J.A.Tainer
Key ref:
Y.Bourne et al. (1996). Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell, 84, 863-874. PubMed id: 8601310 DOI: 10.1016/S0092-8674(00)81065-X
Date:
03-Sep-98     Release date:   09-Sep-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2
Seq:
Struc:
298 a.a.
287 a.a.
Protein chain
Pfam   ArchSchema ?
P61024  (CKS1_HUMAN) -  Cyclin-dependent kinases regulatory subunit 1
Seq:
Struc:
79 a.a.
70 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: E.C.2.7.11.22  - Cyclin-dependent kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ 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   29 terms 
  Biochemical function     nucleotide binding     13 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0092-8674(00)81065-X Cell 84:863-874 (1996)
PubMed id: 8601310  
 
 
Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.
Y.Bourne, M.H.Watson, M.J.Hickey, W.Holmes, W.Rocque, S.I.Reed, J.A.Tainer.
 
  ABSTRACT  
 
The 2.6 Angstrom crystal structure for human cyclin-dependent kinase 2(CDK2) in complex with CksHs1, a human homolog of essential yeast cell cycle-regulatory proteins suc1 and Cks1, reveals that CksHs1 binds via all four beta strands to the kinase C-terminal lobe. This interface is biologically critical, based upon mutational analysis, but far from the CDK2 N-terminal lobe, cyclin, and regulatory phosphorylation sites. CDK2 binds the Cks single domain conformation and interacts with conserved hydrophobic residues plus His-60 and Glu-63 in their closed beta-hinge motif conformation. The beta hinge opening to form the Cks beta-interchanged dimer sterically precludes CDK2 binding, providing a possible mechanism regulating CDK2-Cks interactions. One face of the complex exposes the sequence-conserved phosphate-binding region on Cks and the ATP-binding site on CDK2, suggesting that CKs may target CDK2 to other phosphoproteins during the cell cycle.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Quality of the Structure and Overall View of the CDK2–CksHs1 Complex(A) Stereo view of the 2.6 Å resolution omit Fo–Fc electron density map, contoured at 2σ, showing the predominant cluster of hydrophobic residues forming the binding interface. The coordinates of this region (5% of the total number of atoms) were omitted and the protein coordinates were refined by simulated annealing before the phase calculation. Residues are labeled in white for CDK2 and in yellow for CksHs1.(B) Ribbon diagram of CksHs1 (yellow) bound to CDK2, with the N-lobe in purple and the C-lobe in blue and green. The ATP molecule is displayed at the interface of the two CDK2 lobes (white bonds with red oxygen and blue nitrogen atoms as spheres) and is taken from the free CDK2 coordinates ([11]). The functional structural elements are color coded for CDK2: the β1–β2 loop, red; the disordered loop to the PSTAIRE sequence in helix α1, asterisks; the T loop, white. Side chains forming the phosphorylation sites in the β1–β2 loop (Thr-14 and Tyr-15) and in the T loop (Thr-160) (orange bonds with red oxygen atoms as balls), as well as the CksHs1 side chains forming the conserved phosphate anion–binding site (β1 Lys-11, β2 Arg-20, β3 Trp-54, and β4 Arg-71) (white bonds with blue nitrogen atoms as balls), are displayed. The CDK2 secondary elements involved in the binding interface are highlighted (green), and CksHs1 loops β1–β2 and β3–β4 are labeled L1 and L3, respectively.(C) CksHs1 molecular surface, colored with the residues buried to a 1.6 Å probe radius in pale yellow, the nonburied residues in white, and the phosphate anion–binding site in blue. A ribbon diagram of the CDK2 molecule is shown with the color code and orientation as in (B). A CksHs1 Cα trace (orange) is shown through the surface and reveals that the buried residues cluster in the interior concave face of the CksHs1 β sheet and in the β1–β2 and β3–β4 loops, which envelop the CDK2 helix α5 and loop L14 (green).(D) CDK2 molecular surface, with buried residues in helix α5 (green) and loop L14 (cyan); nonburied residues are shown in white. CksHs1 residues involved in the binding interface are shown (orange bonds with red oxygen, blue nitrogen, and yellow sulfur atoms as balls) with a Cα trace (yellow). CksHs1 residues in all four β strands participate in the binding interface.
Figure 5.
Figure 5. The CDK2–Cyclin A–CksHs1 Ternary Complex(A) Ribbon diagram of a CDK2–cyclin A–CksHs1 complex model based on the coordinates of our CDK2–CksHs1 complex and those of a CDK2–cyclin A complex ([30]) in which the two CDK2 molecules were superimposed based on the Cα atoms of the C-lobe. Besides two distinct binding sites for cyclin A and CksHs1 at the molecular surface of CDK2, this model reveals a large bowl-shaped groove centered around the phosphorylation site at Thr-160 (middle) in the activated conformation of the CDK2 T loop and bordered by cyclin A and CksHs1 molecules. The presence of positively charged residues (Lys-24, Lys-30, and Lys-34 in CksHs1 and Lys-226 and Lys-417 in cyclin A) located on each side of the groove is displayed (purple bonds and blue for nitrogen atoms as balls). The molecules and the functionally important elements in CDK2 are color coded as in Figure 1B, with cyclin A in green. ATP is taken from the CDK2–cyclin A complex coordinates previously described ( [30]).(B) Molecular surface of the CDK2–cyclin A–CksHs1 complex oriented vert, similar 90° away from that in (A), with the same color code. The CksHs1 phosphate anion–binding site (blue) is exposed into the solvent and located on the same side of the CDK2 catalytic site with the ATP molecule bound between the two lobes, thus forming a continuous surface for recognition of a Cdk substrate or other phosphoproteins. The two CksHs1 α helices (orange) are also solvent accessible. The T loop (white), containing the phosphorylation site at position Thr-160 (middle), protrudes at the interface of CksHs1 and cyclin A. Figure 1 and Figure 2 and 2B, 3C, and 4 were generated with the Application Visualization System (AVS) (Advanced Visual Systems, Waltham, Massachusetts), and Figure 1A and Figure 2C were generated with TURBO-FRODO ( [52]). The solvent-accessible surfaces were calculated with MS ( [9]), and the ribbon diagrams were generated using RIBBONS ( [8]) implemented in AVS.
 
  The above figures are reprinted by permission from Cell Press: Cell (1996, 84, 863-874) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19228269 A.Krishnan, S.A.Nair, and M.R.Pillai (2010).
Loss of cks1 homeostasis deregulates cell division cycle.
  J Cell Mol Med, 14, 154-164.  
20733051 B.Di Fiore, and J.Pines (2010).
How cyclin A destruction escapes the spindle assembly checkpoint.
  J Cell Biol, 190, 501-509.  
20482653 D.G.Srinivasan, B.Fenton, S.Jaubert-Possamai, and M.Jaouannet (2010).
Analysis of meiosis and cell cycle genes of the facultatively asexual pea aphid, Acyrthosiphon pisum (Hemiptera: Aphididae).
  Insect Mol Biol, 19, 229-239.  
20516216 R.Holic, A.Kukalev, S.Lane, E.J.Andress, I.Lau, C.W.Yu, M.J.Edelmann, B.M.Kessler, and V.P.Yu (2010).
Cks1 activates transcription by binding to the ubiquitylated proteasome.
  Mol Cell Biol, 30, 3894-3901.  
20421461 S.S.Taylor, and A.P.Kornev (2010).
Yet another "active" pseudokinase, Erb3.
  Proc Natl Acad Sci U S A, 107, 8047-8048.  
20596523 S.V.Del Rincón, J.Rogers, M.Widschwendter, D.Sun, H.B.Sieburg, and C.Spruck (2010).
Development and validation of a method for profiling post-translational modification activities using protein microarrays.
  PLoS One, 5, e11332.  
19566963 B.T.Tobe, A.A.Kitazono, J.S.Garcia, R.A.Gerber, B.J.Bevis, J.S.Choy, D.Chasman, and S.J.Kron (2009).
Morphogenesis signaling components influence cell cycle regulation by cyclin dependent kinase.
  Cell Div, 4, 12.  
19501598 J.J.Perry, R.M.Harris, D.Moiani, A.J.Olson, and J.A.Tainer (2009).
p38alpha MAP kinase C-terminal domain binding pocket characterized by crystallographic and computational analyses.
  J Mol Biol, 391, 1.
PDB code: 3hvc
18691976 H.Daub, J.V.Olsen, M.Bairlein, F.Gnad, F.S.Oppermann, R.Körner, Z.Greff, G.Kéri, O.Stemmann, and M.Mann (2008).
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
  Mol Cell, 31, 438-448.  
18625720 H.S.Martinsson-Ahlzén, V.Liberal, B.Grünenfelder, S.R.Chaves, C.H.Spruck, and S.I.Reed (2008).
Cyclin-dependent kinase-associated proteins Cks1 and Cks2 are essential during early embryogenesis and for cell cycle progression in somatic cells.
  Mol Cell Biol, 28, 5698-5709.  
19119325 J.Nilmeier, and M.Jacobson (2008).
Multiscale Monte Carlo Sampling of Protein Sidechains: Application to Binding Pocket Flexibility.
  J Chem Theory Comput, 4, 835-846.  
18471975 R.Wolthuis, L.Clay-Farrace, W.van Zon, M.Yekezare, L.Koop, J.Ogink, R.Medema, and J.Pines (2008).
Cdc20 and Cks direct the spindle checkpoint-independent destruction of cyclin A.
  Mol Cell, 30, 290-302.  
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.  
17299750 I.Kufareva, L.Budagyan, E.Raush, M.Totrov, and R.Abagyan (2007).
PIER: protein interface recognition for structural proteomics.
  Proteins, 67, 400-417.  
17585314 J.A.Ubersax, and J.E.Ferrell (2007).
Mechanisms of specificity in protein phosphorylation.
  Nat Rev Mol Cell Biol, 8, 530-541.  
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.  
17409098 S.Xu, M.Abbasian, P.Patel, K.Jensen-Pergakes, C.R.Lombardo, B.E.Cathers, W.Xie, F.Mercurio, M.Pagano, D.Giegel, and S.Cox (2007).
Substrate recognition and ubiquitination of SCFSkp2/Cks1 ubiquitin-protein isopeptide ligase.
  J Biol Chem, 282, 15462-15470.  
18047746 T.Cardozo, and M.Pagano (2007).
Wrenches in the works: drug discovery targeting the SCF ubiquitin ligase and APC/C complexes.
  BMC Biochem, 8, S9.  
16343905 M.Shirayama, M.C.Soto, T.Ishidate, S.Kim, K.Nakamura, Y.Bei, S.van den Heuvel, and C.C.Mello (2006).
The Conserved Kinases CDK-1, GSK-3, KIN-19, and MBK-2 Promote OMA-1 Destruction to Regulate the Oocyte-to-Embryo Transition in C. elegans.
  Curr Biol, 16, 47-55.  
16774918 P.Ji, L.Goldin, H.Ren, D.Sun, D.Guardavaccaro, M.Pagano, and L.Zhu (2006).
Skp2 contains a novel cyclin A binding domain that directly protects cyclin A from inhibition by p27Kip1.
  J Biol Chem, 281, 24058-24069.  
16209941 B.Hao, N.Zheng, B.A.Schulman, G.Wu, J.J.Miller, M.Pagano, and N.P.Pavletich (2005).
Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase.
  Mol Cell, 20, 9.
PDB codes: 2ass 2ast
15772084 M.A.Seeliger, M.Spichty, S.E.Kelly, M.Bycroft, S.M.Freund, M.Karplus, and L.S.Itzhaki (2005).
Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins.
  J Biol Chem, 280, 30448-30459.  
16170306 N.J.Pearson, C.F.Cullen, N.S.Dzhindzhev, and H.Ohkura (2005).
A pre-anaphase role for a Cks/Suc1 in acentrosomal spindle formation of Drosophila female meiosis.
  EMBO Rep, 6, 1058-1063.  
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
15629725 V.P.Yu, C.Baskerville, B.Grünenfelder, and S.I.Reed (2005).
A kinase-independent function of Cks1 and Cdk1 in regulation of transcription.
  Mol Cell, 17, 145-151.  
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.  
15175336 S.Araki, M.Ito, T.Soyano, R.Nishihama, and Y.Machida (2004).
Mitotic cyclins stimulate the activity of c-Myb-like factors for transactivation of G2/M phase-specific genes in tobacco.
  J Biol Chem, 279, 32979-32988.  
  15579456 S.Kitajima, Y.Kudo, I.Ogawa, T.Bashir, M.Kitagawa, M.Miyauchi, M.Pagano, and T.Takata (2004).
Role of Cks1 overexpression in oral squamous cell carcinomas: cooperation with Skp2 in promoting p27 degradation.
  Am J Pathol, 165, 2147-2155.  
15340381 T.Cardozo, and M.Pagano (2004).
The SCF ubiquitin ligase: insights into a molecular machine.
  Nat Rev Mol Cell Biol, 5, 739-751.  
14506247 F.L.Chou, J.M.Hill, J.C.Hsieh, J.Pouyssegur, A.Brunet, A.Glading, F.Uberall, J.W.Ramos, M.H.Werner, and M.H.Ginsberg (2003).
PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.
  J Biol Chem, 278, 52587-52597.  
12897769 M.A.Seeliger, S.E.Breward, A.Friedler, O.Schon, and L.S.Itzhaki (2003).
Cooperative organization in a macromolecular complex.
  Nat Struct Biol, 10, 718-724.  
12827207 M.C.Morris, P.Kaiser, S.Rudyak, C.Baskerville, M.H.Watson, and S.I.Reed (2003).
Cks1-dependent proteasome recruitment and activation of CDC20 transcription in budding yeast.
  Nature, 423, 1009-1013.  
  18629088 P.Aloy, and R.B.Russell (2003).
Understanding and Predicting Protein Assemblies With 3D Structures.
  Comp Funct Genomics, 4, 410-415.  
12554650 R.Dajani, E.Fraser, S.M.Roe, M.Yeo, V.M.Good, V.Thompson, T.C.Dale, and L.H.Pearl (2003).
Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex.
  EMBO J, 22, 494-501.
PDB code: 1o9u
14622140 T.Hattori, K.Kitagawa, C.Uchida, T.Oda, and M.Kitagawa (2003).
Cks1 is degraded via the ubiquitin-proteasome pathway in a cell cycle-dependent manner.
  Genes Cells, 8, 889-896.  
14502991 W.Dewitte, and J.A.Murray (2003).
The plant cell cycle.
  Annu Rev Plant Biol, 54, 235-264.  
12813041 W.Wang, D.Ungermannova, L.Chen, and X.Liu (2003).
A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1.
  J Biol Chem, 278, 32390-32396.  
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.  
11812792 B.Odaert, I.Landrieu, K.Dijkstra, G.Schuurman-Wolters, P.Casteels, J.M.Wieruszeski, D.Inze, R.Scheek, and G.Lippens (2002).
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
  J Biol Chem, 277, 12375-12381.  
12140288 D.Sitry, M.A.Seeliger, T.K.Ko, D.Ganoth, S.E.Breward, L.S.Itzhaki, M.Pagano, and A.Hershko (2002).
Three different binding sites of Cks1 are required for p27-ubiquitin ligation.
  J Biol Chem, 277, 42233-42240.  
12435635 D.Tedesco, J.Lukas, and S.I.Reed (2002).
The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2).
  Genes Dev, 16, 2946-2957.  
12079670 E.A.Oakenfull, C.Riou-Khamlichi, and J.A.Murray (2002).
Plant D-type cyclins and the control of G1 progression.
  Philos Trans R Soc Lond B Biol Sci, 357, 749-760.  
11959850 M.C.Morris, C.Gondeau, J.A.Tainer, and G.Divita (2002).
Kinetic mechanism of activation of the Cdk2/cyclin A complex. Key role of the C-lobe of the Cdk.
  J Biol Chem, 277, 23847-23853.  
11839489 M.E.Newcomer (2002).
Protein folding and three-dimensional domain swapping: a strained relationship?
  Curr Opin Struct Biol, 12, 48-53.  
12468233 P.Aloy, and R.B.Russell (2002).
The third dimension for protein interactions and complexes.
  Trends Biochem Sci, 27, 633-638.  
11506705 C.Ellenrieder, B.Bartosch, G.Y.Lee, M.Murphy, C.Sweeney, M.Hergersberg, M.Carrington, R.Jaussi, and T.Hunt (2001).
The long form of CDK2 arises via alternative splicing and forms an active protein kinase with cyclins A and E.
  DNA Cell Biol, 20, 413-423.  
11463388 C.Spruck, H.Strohmaier, M.Watson, A.P.Smith, A.Ryan, T.W.Krek, and S.I.Reed (2001).
A CDK-independent function of mammalian Cks1: targeting of SCF(Skp2) to the CDK inhibitor p27Kip1.
  Mol Cell, 7, 639-650.  
11527976 E.Ceccarelli, and C.Mann (2001).
A Cdc28 mutant uncouples G1 cyclin phosphorylation and ubiquitination from G1 cyclin proteolysis.
  J Biol Chem, 276, 41725-41732.  
11463386 H.Song, N.Hanlon, N.R.Brown, M.E.Noble, L.N.Johnson, and D.Barford (2001).
Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2.
  Mol Cell, 7, 615-626.
PDB codes: 1fpz 1fq1
11516665 J.W.Harper (2001).
Protein destruction: adapting roles for Cks proteins.
  Curr Biol, 11, R431-R435.  
11573096 J.W.Schymkowitz, F.Rousseau, H.R.Wilkinson, A.Friedler, and L.S.Itzhaki (2001).
Observation of signal transduction in three-dimensional domain swapping.
  Nat Struct Biol, 8, 888-892.  
11574463 K.Niefind, B.Guerra, I.Ermakowa, and O.G.Issinger (2001).
Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
  EMBO J, 20, 5320-5331.
PDB code: 1jwh
11319029 L.De Veylder, G.T.Beemster, T.Beeckman, and D.Inzé (2001).
CKS1At overexpression in Arabidopsis thaliana inhibits growth by reducing meristem size and inhibiting cell-cycle progression.
  Plant J, 25, 617-626.  
11722776 M.B.Boniotti, and C.Gutierrez (2001).
A cell-cycle-regulated kinase activity phosphorylates plant retinoblastoma protein and contains, in Arabidopsis, a CDKA/cyclin D complex.
  Plant J, 28, 341-350.  
12030783 S.Wadler (2001).
Perspectives for cancer therapies with cdk2 inhibitors.
  Drug Resist Updat, 4, 347-367.  
10673427 D.O.Alonso, E.Alm, and V.Daggett (2000).
Characterization of the unfolding pathway of the cell-cycle protein p13suc1 by molecular dynamics simulations: implications for domain swapping.
  Structure, 8, 101-110.  
10913169 G.J.Reynard, W.Reynolds, R.Verma, and R.J.Deshaies (2000).
Cks1 is required for G(1) cyclin-cyclin-dependent kinase activity in budding yeast.
  Mol Cell Biol, 20, 5858-5864.  
10673431 J.W.Schymkowitz, F.Rousseau, L.R.Irvine, and L.S.Itzhaki (2000).
The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping.
  Structure, 8, 89.  
10637334 T.K.Albert, M.Lemaire, N.L.van Berkum, R.Gentz, M.A.Collart, and H.T.Timmers (2000).
Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits.
  Nucleic Acids Res, 28, 809-817.  
10997903 Y.Bourne, M.H.Watson, A.S.Arvai, S.L.Bernstein, S.I.Reed, and J.A.Tainer (2000).
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.
  Structure, 8, 841-850.
PDB code: 1qb3
10601234 D.Patra, S.X.Wang, A.Kumagai, and W.G.Dunphy (1999).
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
  J Biol Chem, 274, 36839-36842.  
10360827 I.Urbanowicz-Kachnowicz, N.Baghdassarian, C.Nakache, D.Gracia, Y.Mekki, P.A.Bryon, and M.Ffrench (1999).
ckshs expression is linked to cell proliferation in normal and malignant human lymphoid cells.
  Int J Cancer, 82, 98.  
10607671 J.A.Endicott, M.E.Noble, and J.A.Tucker (1999).
Cyclin-dependent kinases: inhibition and substrate recognition.
  Curr Opin Struct Biol, 9, 738-744.  
10447673 L.Détivaud, G.R.Pettit, and L.Meijer (1999).
Characterization of a novel cdk1-related kinase.
  Eur J Biochem, 264, 55-66.  
  10323869 P.Kaiser, V.Moncollin, D.J.Clarke, M.H.Watson, B.L.Bertolaet, S.I.Reed, and E.Bailly (1999).
Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets.
  Genes Dev, 13, 1190-1202.  
10092646 P.Sharma, P.J.Steinbach, M.Sharma, N.D.Amin, J.J.Barchi, and H.C.Pant (1999).
Identification of substrate binding site of cyclin-dependent kinase 5.
  J Biol Chem, 274, 9600-9606.  
  9716407 D.Patra, and W.G.Dunphy (1998).
Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosis.
  Genes Dev, 12, 2549-2559.  
  9632748 E.A.Egan, and M.J.Solomon (1998).
Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.
  Mol Cell Biol, 18, 3659-3667.  
9760264 M.C.Morris, F.Heitz, and G.Divita (1998).
Kinetics of dimerization and interactions of p13suc1 with cyclin-dependent kinases.
  Biochemistry, 37, 14257-14266.  
  9841670 M.D.Mendenhall, and A.E.Hodge (1998).
Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.
  Microbiol Mol Biol Rev, 62, 1191-1243.  
  9774639 M.L.Hixon, A.I.Flores, M.W.Wagner, and A.Gualberto (1998).
Ectopic expression of cdc2/cdc28 kinase subunit Homo sapiens 1 uncouples cyclin B metabolism from the mitotic spindle cell cycle checkpoint.
  Mol Cell Biol, 18, 6224-6237.  
9425343 A.Hershko (1997).
Roles of ubiquitin-mediated proteolysis in cell cycle control.
  Curr Opin Cell Biol, 9, 788-799.  
9442875 D.O.Morgan (1997).
Cyclin-dependent kinases: engines, clocks, and microprocessors.
  Annu Rev Cell Dev Biol, 13, 261-291.  
9125522 F.Heitz, M.C.Morris, D.Fesquet, J.C.Cavadore, M.Dorée, and G.Divita (1997).
Interactions of cyclins with cyclin-dependent kinases: a common interactive mechanism.
  Biochemistry, 36, 4995-5003.  
  9042920 K.Saar, K.H.Chrzanowska, M.Stumm, M.Jung, G.Nürnberg, T.F.Wienker, E.Seemanová, R.D.Wegner, A.Reis, and K.Sperling (1997).
The gene for the ataxia-telangiectasia variant, Nijmegen breakage syndrome, maps to a 1-cM interval on chromosome 8q21.
  Am J Hum Genet, 60, 605-610.  
9095200 L.Tong, S.Pav, D.M.White, S.Rogers, K.M.Crane, C.L.Cywin, M.L.Brown, and C.A.Pargellis (1997).
A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket.
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PDB code: 1ian
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Binding of activated cyclosome to p13(suc1). Use for affinity purification.
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8939669 D.O.Morgan (1996).
The dynamics of cyclin dependent kinase structure.
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8944769 J.L.Li, K.J.Robson, J.L.Chen, G.A.Targett, and D.A.Baker (1996).
Pfmrk, a MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization.
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8939596 J.Pines (1996).
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