1BUH

CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITH CELL CYCLE-REGULATORY PROTEIN CKSHS1

Summary for 1BUH

• Entry DOI: 10.2210/pdb1buh/pdb
• Descriptor: PROTEIN (CDK2 HUMAN), PROTEIN (CKSHS1 HUMAN) (3 entities in total)
• Functional Keywords: transferase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 43655.70

Authors

Bourne, Y.,Tainer, J.A. (deposition date: 1998-09-03, release date: 1998-09-09, Last modification date: 2024-04-03)

Primary citation

Bourne, Y.,Watson, M.H.,Hickey, M.J.,Holmes, W.,Rocque, W.,Reed, S.I.,Tainer, J.A.
Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.
Cell(Cambridge,Mass.), 84:863-874, 1996

PubMed Abstract: The 2.6 Angstrom crystal structure for human cyclin-dependent kinase 2(CDK2) in complex with CksHs1, a human homolog of essential yeast cell cycle-regulatory proteins suc1 and Cks1, reveals that CksHs1 binds via all four beta strands to the kinase C-terminal lobe. This interface is biologically critical, based upon mutational analysis, but far from the CDK2 N-terminal lobe, cyclin, and regulatory phosphorylation sites. CDK2 binds the Cks single domain conformation and interacts with conserved hydrophobic residues plus His-60 and Glu-63 in their closed beta-hinge motif conformation. The beta hinge opening to form the Cks beta-interchanged dimer sterically precludes CDK2 binding, providing a possible mechanism regulating CDK2-Cks interactions. One face of the complex exposes the sequence-conserved phosphate-binding region on Cks and the ATP-binding site on CDK2, suggesting that CKs may target CDK2 to other phosphoproteins during the cell cycle.

PubMed: 8601310
DOI: 10.1016/S0092-8674(00)81065-X

Experimental method

X-RAY DIFFRACTION (2.6 Å)