细胞周期蛋白A-CDK2复合物结构揭示的CDK激活机制
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.
作者信息
Jeffrey P D, Russo A A, Polyak K, Gibbs E, Hurwitz J, Massagué J, Pavletich N P
机构信息
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
出版信息
Nature. 1995 Jul 27;376(6538):313-20. doi: 10.1038/376313a0.
The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A 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.
人细胞周期蛋白A-细胞周期蛋白依赖性激酶2（CDK2）-ATP复合物的晶体结构已在2.3埃分辨率下确定。细胞周期蛋白A结合到CDK2催化裂隙的一侧，诱导其PSTAIRE螺旋和T环发生大的构象变化。这些变化通过重新排列活性位点残基并解除催化裂隙入口处的空间位阻来激活激酶。
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