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1buh

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1buh, resolution 2.60Å ()

Domains:

S_TKc, S_TKc, CKS

Structural annotation:
Resources:	CATH : 1Buha02, 1Buha01, 1Buhb00 InterPro : Ipr002290, Ipr011009, Ipr008271, Ipr000719, Ipr000789 Pfam : PF00069, PF01111 SCOP : d1buha_, d1buhb_ UniProt : P24941, P61024

Functional annotation:
Resources:	GeneCard : CDK2, CKS1B
Cellular component:	cytoplasm nucleus
Biological process:	positive regulation of cell proliferation cell cycle mitosis regulation of DNA replication cell division protein amino acid phosphorylation G2/M transition of mitotic cell cycle traversing start control point of mitotic cell cycle regulation of cyclin-dependent protein kinase activity cell proliferation
Molecular function:	nucleotide binding ATP binding protein serine/threonine kinase activity protein kinase activity protein binding cyclin-dependent protein kinase activity kinase activity transferase activity identical protein binding cyclin-dependent protein kinase regulator activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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

Publication Abstract from PubMed

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.

Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1., Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA, Cell. 1996 Mar 22;84(6):863-74. PMID:8601310

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1BUH is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell. 1996 Mar 22;84(6):863-74. PMID:8601310

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