PubMed:7630397 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":59,"end":66},"obj":"protein"},{"id":"T2","span":{"begin":67,"end":71},"obj":"protein"},{"id":"T3","span":{"begin":116,"end":123},"obj":"protein"},{"id":"T4","span":{"begin":124,"end":148},"obj":"protein"},{"id":"T5","span":{"begin":150,"end":154},"obj":"protein"},{"id":"T6","span":{"begin":238,"end":242},"obj":"protein"}],"text":"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.\nThe 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."}