From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1qb3.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1qb3.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }} | | {{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1'''
| + | ===CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | BACKGROUND: 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. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10997903}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10997903 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10997903}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Cell cycle mutagenesis domain swapping]] | | [[Category: Cell cycle mutagenesis domain swapping]] |
| | [[Category: Cyclin-dependent kinase]] | | [[Category: Cyclin-dependent kinase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:31:54 2008'' |
Revision as of 14:31, 27 July 2008
Template:STRUCTURE 1qb3
CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1
Template:ABSTRACT PUBMED 10997903
About this Structure
1QB3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions., Bourne Y, Watson MH, Arvai AS, Bernstein SL, Reed SI, Tainer JA, Structure. 2000 Aug 15;8(8):841-50. PMID:10997903
Page seeded by OCA on Sun Jul 27 17:31:54 2008
