TI  - Mechanism of CDK activation revealed by the structure of a  <prot>cyclinA</prot> - <prot>CDK2</prot> 
      complex.
PG  - 313-20
AB  - The crystal structure of the human  <prot>cyclinA</prot> - <prot>cyclin-dependent kinase2</prot>
      (<prot>CDK2</prot>) -ATP complex has been determined at 2.3 A resolution.  CyclinA  binds
      to one side of  <prot>CDK2</prot> '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.
AD  - Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering
