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PDBsum entry 2jgz

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protein Protein-protein interface(s) links
Transferase PDB id
2jgz
Jmol
Contents
Protein chains
289 a.a. *
260 a.a. *
Waters ×5
* Residue conservation analysis
PDB id:
2jgz
Name: Transferase
Title: Crystal structure of phospho-cdk2 in complex with cyclin b
Structure: Cell division protein kinase 2. Chain: a. Fragment: residues 1-288. Synonym: p33 protein kinase. Engineered: yes. Other_details: phosphorylated on thr160. G2/mitotic-specific cyclin-b1. Chain: b. Fragment: residues 167-426.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Resolution:
2.90Å     R-factor:   0.208     R-free:   0.275
Authors: N.R.Brown,E.Petri,E.D.Lowe,V.Skamnaki,L.N.Johnson
Key ref: N.R.Brown et al. (2007). Cyclin B and cyclin A confer different substrate recognition properties on CDK2. Cell Cycle, 6, 1350-1359. PubMed id: 17495531
Date:
17-Feb-07     Release date:   22-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2
Seq:
Struc:
298 a.a.
289 a.a.*
Protein chain
Pfam   ArchSchema ?
P14635  (CCNB1_HUMAN) -  G2/mitotic-specific cyclin-B1
Seq:
Struc:
433 a.a.
260 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: 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    
 
 
Cell Cycle 6:1350-1359 (2007)
PubMed id: 17495531  
 
 
Cyclin B and cyclin A confer different substrate recognition properties on CDK2.
N.R.Brown, E.D.Lowe, E.Petri, V.Skamnaki, R.Antrobus, L.N.Johnson.
 
  ABSTRACT  
 
The transitions of the cell cycle are regulated by the cyclin dependent protein kinases (CDKs). The cyclins activate their respective CDKs and confer substrate recognition properties. We report the structure of phospho-CDK2/cyclin B and show that cyclin B confers M phase-like properties on CDK2, the kinase that is usually associated with S phase. Cyclin B produces an almost identical activated conformation of CDK2 as that produced by cyclin A. There are differences between cyclin A and cyclin B at the recruitment site, which in cyclin A is used to recruit substrates containing an RXL motif. Because of sequence differences this site in cyclin B binds RXL motifs more weakly than in cyclin A. Despite similarity in kinase structures, phospho-CDK2/cyclin B phosphorylates substrates, such as nuclear lamin and a model peptide derived from p107, at sequences SPXX that differ from the canonical CDK2/cyclin A substrate recognition motif, SPXK. CDK2/cyclin B phosphorylation at these non-canonical sites is not dependent on the presence of a RXL recruitment motif. The p107 peptide contains two SP motifs each followed by a non-canonical sequence of which only one site (Ser640) is phosphorylated by pCDK2/cyclin A while two sites are phosphorylated by pCDK2/cyclin B. The second site is too close to the RXL motif to allow the cyclin A recruitment site to be effective, as previous work has shown that there must be at least 16 residues between the catalytic site serine and the RXL motif. Thus the cyclins A and B in addition to their role in promoting the activatory conformational switch in CDK2, also provide differential substrate specificity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21358637 Y.Wang, J.C.Fisher, R.Mathew, L.Ou, S.Otieno, J.Sublet, L.Xiao, J.Chen, M.F.Roussel, and R.W.Kriwacki (2011).
Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21.
  Nat Chem Biol, 7, 214-221.  
20639412 A.Ofir, and D.Kornitzer (2010).
Candida albicans cyclin Clb4 carries S-phase cyclin activity.
  Eukaryot Cell, 9, 1311-1319.  
19858290 C.Li, M.Andrake, R.Dunbrack, and G.H.Enders (2010).
A bifunctional regulatory element in human somatic Wee1 mediates cyclin A/Cdk2 binding and Crm1-dependent nuclear export.
  Mol Cell Biol, 30, 116-130.  
19472269 G.Kontopidis, M.J.Andrews, C.McInnes, A.Plater, L.Innes, S.Renachowski, A.Cowan, and P.M.Fischer (2009).
Truncation and optimisation of peptide inhibitors of cyclin-dependent kinase 2-cyclin a through structure-guided design.
  ChemMedChem, 4, 1120-1128.
PDB codes: 2wev 2wfy 2whb
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.
  Proc Natl Acad Sci U S A, 106, 4171-4176.
PDB code: 3g33
18951089 E.J.Ruiz, T.Hunt, and A.R.Nebreda (2008).
Meiotic inactivation of Xenopus Myt1 by CDK/XRINGO, but not CDK/cyclin, via site-specific phosphorylation.
  Mol Cell, 32, 210-220.  
18184589 J.Eswaran, A.Bernad, J.M.Ligos, B.Guinea, J.E.Debreczeni, F.Sobott, S.A.Parker, R.Najmanovich, B.E.Turk, and S.Knapp (2008).
Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture.
  Structure, 16, 115-124.  
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.
  EMBO J, 27, 1907-1918.
PDB codes: 2ivx 3blh 3blq 3blr
17881737 A.M.Bentley, G.Normand, J.Hoyt, and R.W.King (2007).
Distinct sequence elements of cyclin B1 promote localization to chromatin, centrosomes, and kinetochores during mitosis.
  Mol Biol Cell, 18, 4847-4858.  
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.