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

被引：1222

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

来源：

NATURE | 1995年 / 376卷 / 6538期

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

页码：313 / 320

页数：8

共 50 条

[1]

BRUNGER AT, 1991, XPLOR SYSTEM CRYSTAL

[2] PHOSPHORYLATION INDEPENDENT ACTIVATION OF HUMAN CYCLIN-DEPENDENT KINASE-2 BY CYCLIN-A INVITRO [J].