1QB3

CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1

Summary for 1QB3

• Entry DOI: 10.2210/pdb1qb3/pdb
• Descriptor: CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT (2 entities in total)
• Functional Keywords: cell cycle mutagenesis domain swapping, cyclin-dependent kinase, cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 3
• Total formula weight: 53450.15

Authors

Bourne, Y.,Watson, M.H.,Arvai, A.S.,Bernstein, S.L.,Reed, S.I.,Tainer, J.A. (deposition date: 1999-04-30, release date: 2000-08-31, Last modification date: 2024-10-30)

Primary citation

Bourne, Y.,Watson, M.H.,Arvai, A.S.,Bernstein, S.L.,Reed, S.I.,Tainer, J.A.
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.
Structure Fold.Des., 8:841-850, 2000

PubMed Abstract: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif.

PubMed: 10997903
DOI: 10.1016/S0969-2126(00)00175-1

Experimental method

X-RAY DIFFRACTION (3 Å)