1JST

PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A

Summary for 1JST

• Entry DOI: 10.2210/pdb1jst/pdb
• Descriptor: CYCLIN-DEPENDENT KINASE-2, CYCLIN A, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: complex (protein kinase-cyclin), cyclin, cdk, phosphorylation, complex (protein kinase-cyclin) complex, complex (protein kinase/cyclin)
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P20248
• Total number of polymer chains: 4
• Total formula weight: 128485.77

Authors

Russo, A.A.,Jeffrey, P.D.,Pavletich, N.P. (deposition date: 1996-07-03, release date: 1997-01-11, Last modification date: 2024-11-20)

Primary citation

Russo, A.A.,Jeffrey, P.D.,Pavletich, N.P.
Structural basis of cyclin-dependent kinase activation by phosphorylation.
Nat.Struct.Biol., 3:696-700, 1996

PubMed Abstract: Cyclin-dependent kinase (CDK)-cyclin complexes require phosphorylation on the CDK subunit for full activation of their Ser/Thr protein kinase activity. The crystal structure of the phosphorylated CDK2-CyclinA-ATP gamma S complex has been determined at 2.6 A resolution. The phosphate group, which is on the regulatory T-loop of CDK2, is mostly buried, its charge being neutralized by three Arg side chains. The arginines help extend the influence of the phosphate group through a network of hydrogen bonds to both CDK2 and cyclinA. Comparison with the unphosphorylated CDK2-CyclinA complex shows that the T-loop moves by as much as 7 A, and this affects the putative substrate binding site as well as resulting in additional CDK2-CyclinA contacts. The phosphate group thus acts as a major organizing centre in the CDK2-CyclinA complex.

PubMed: 8756328
DOI: 10.1038/nsb0896-696

Experimental method

X-RAY DIFFRACTION (2.6 Å)