Russo A A, Jeffrey P D, Patten A K, Massagué J, Pavletich N P
Cellular Biochemistry and Biophysics Program, Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.
Nature. 1996 Jul 25;382(6589):325-31. doi: 10.1038/382325a0.
The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 angstrom. p27Kip1 binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.
已确定与磷酸化细胞周期蛋白A - 细胞周期蛋白依赖性激酶2(Cdk2)复合物结合的人p27Kip1激酶抑制结构域的晶体结构,分辨率为2.3埃。p27Kip1以一种延伸结构与细胞周期蛋白A和Cdk2相互作用的方式结合该复合物。在细胞周期蛋白A上,它结合在由保守的细胞周期蛋白盒残基形成的凹槽中。在Cdk2上,它结合并重新排列氨基末端叶,还插入催化裂隙,模拟ATP。