MECHANISM OF CDK ACTIVATION REVEALED BY THE STRUCTURE OF A CYCLINA-CDK2 COMPLEX

Citation
Pd. Jeffrey et al., MECHANISM OF CDK ACTIVATION REVEALED BY THE STRUCTURE OF A CYCLINA-CDK2 COMPLEX, Nature, 376(6538), 1995, pp. 313-320
Citations number
50
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
376
Issue
6538
Year of publication
1995
Pages
313 - 320
Database
ISI
SICI code
0028-0836(1995)376:6538<313:MOCARB>2.0.ZU;2-G
Abstract
The crystal structure of the human cyclinA-cyclin-dependent kinase2 (C DK2)-ATP complex has been determined at 2.3 Angstrom resolution. Cycli nA binds to one side of CDK2's catalytic cleft, inducing large conform ational changes in its PSTAIRE helix and T-loop. These changes activat e the kinase by realigning active site residues and relieving the ster ic blockade at the entrance of the catalytic cleft.