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MECHANISM OF CDK ACTIVATION REVEALED BY THE STRUCTURE OF A CYCLINA-CDK2 COMPLEX
Author(s): JEFFREY PD, RUSO AA, POLYAK K, GIBBS E, HURWITZ J, MASSAGUE J, PAVLETICH NP
Source: NATURE    Volume: 376    Issue: 6538    Pages: 313-320    Published: JUL 27 1995  
Times Cited: 787     References: 50     
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.
Document Type: Article
Language: English
Reprint Address: JEFFREY, PD (reprint author), MEM SLOAN KETTERING CANC CTR, CELLULAR BIOCHEM & BIOPHYS PROGRAM, 1275 YORK AVE, NEW YORK, NY 10021 USA
Addresses:
1. MEM SLOAN KETTERING CANC CTR, CELL BIOL & GENET PROGRAM, NEW YORK, NY 10021 USA
2. MEM SLOAN KETTERING CANC CTR, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA
3. MEM SLOAN KETTERING CANC CTR, PROGRAM MOLEC BIOL, NEW YORK, NY 10021 USA
Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF
Subject Category: Multidisciplinary Sciences
IDS Number: RL443
ISSN: 0028-0836
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