Crystal structure of the p27(Kip1) cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex Journal Article

  


Authors: Russo, A. A.; Jeffrey, P. D.; Patten, A. K.; Massagué, J.; Pavletich, N. P.
Article Title: Crystal structure of the p27(Kip1) cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
Abstract: The crystal structure of the human p27(Kip1) kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 Å. p27(Kip1) binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.
Keywords: molecular genetics; binding affinity; protein domain; cell cycle protein; metabolism; cell cycle proteins; complex formation; enzyme inhibition; protein binding; enzyme inhibitor; protein serine threonine kinase; phosphorylation; chemistry; drug antagonism; amino acid sequence; conserved sequence; molecular sequence data; amino terminal sequence; enzyme inhibitors; protein-serine-threonine kinases; cyclin dependent kinase inhibitor 1b; nucleotide sequence; cyclin-dependent kinase inhibitor p27; tumor suppressor proteins; binding site; crystal structure; hydrogen bond; crystallography, x-ray; binding sites; conformational transition; adenosine triphosphate; cycline; x ray crystallography; tumor suppressor protein; cyclin-dependent kinases; cyclins; cyclin a; cyclin dependent kinase; enzyme substrate complex; crystallography; cyclin dependent kinase 2; cyclin-dependent kinase 2; microtubule-associated proteins; microtubule associated protein; cdk2 protein, human; enzyme inhibitor complex; cdc2-cdc28 kinases; humans; human; priority journal; article
Journal Title: Nature
Volume: 382
Issue: 6589
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1996-07-25
Start Page: 325
End Page: 331
Language: English
DOI: 10.1038/382325a0
PUBMED: 8684460
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029665852&doi=10.1038%2f382325a0&partnerID=40&md5=7ce6765896d35520962452946b050c97
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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MSK Authors
  1. Philip D Jeffrey
    30 Jeffrey
  2. Alicia A R Russo
    12 Russo
  3. Nikola P Pavletich
    85 Pavletich
  4. Joan Massague
    388 Massague
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