Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex Journal Article

  


Authors: Jeffrey, P. D.; Russo, A. A.; Polyak, K.; Gibbs, E.; Hurwitz, J.; Massagué, J.; Pavletich, N. P.
Article Title: Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Abstract: The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 Angstrom resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.
Keywords: phosphorylation; yeast; cyclins; binding; program; crystal-structure; localization; dependent protein-kinase; invitro; catalytic subunit
Journal Title: Nature
Volume: 376
Issue: 6538
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1995-07-27
Start Page: 313
End Page: 320
Language: English
ACCESSION: WOS:A1995RL44300040
DOI: 10.1038/376313a0
PROVIDER: wos
PUBMED: 7630397
Notes: Article -- Source: Wos
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MSK Authors
  1. Philip D Jeffrey
    30 Jeffrey
  2. Alicia A R Russo
    12 Russo
  3. Jerard Hurwitz
    206 Hurwitz
  4. Nikola P Pavletich
    85 Pavletich
  5. Joan Massague
    389 Massague
  6. Kornelia Polyak
    12 Polyak
  7. Emma Gibbs
    14 Gibbs
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