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

被引:1210
作者
JEFFREY, PD
RUSO, AA
POLYAK, K
GIBBS, E
HURWITZ, J
MASSAGUE, J
PAVLETICH, NP
机构
[1] MEM SLOAN KETTERING CANC CTR,CELL BIOL & GENET PROGRAM,NEW YORK,NY 10021
[2] MEM SLOAN KETTERING CANC CTR,HOWARD HUGHES MED INST,NEW YORK,NY 10021
[3] MEM SLOAN KETTERING CANC CTR,PROGRAM MOLEC BIOL,NEW YORK,NY 10021
关键词
D O I
10.1038/376313a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:313 / 320
页数:8
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