1dks: Difference between revisions
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'''CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 IN COMPLEX WITH PHOSPHATE'''<br /> | '''CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 IN COMPLEX WITH PHOSPHATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1DKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1DKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: cell division]] | [[Category: cell division]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:40:17 2008'' | ||
Revision as of 16:40, 15 February 2008
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CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 IN COMPLEX WITH PHOSPHATE
OverviewOverview
The structure of the human CksHs1 homolog of the yeast cell-cycle, regulatory proteins suc1 and CKS1, which bind to the catalytic subunit of, the cyclin-dependent kinases (Cdks) and are essential for yeast cell-cycle, progression in vivo, has been determined at 2.9 A resolution. The CksHs1, single polypeptide domain fold, which consists of a four-stranded, beta-sheet flanked by two alpha-helices, is dramatically different from, the subunit conformation and assembly of the homologous CksHs2, but, strikingly similar to the Cdk N-lobe domain fold. The CksHs1 structure, identifies sequence-conserved residues Glu61 to His65 as a novel, beta-hinge region that folds back to form a beta-hairpin with CksHs1, subunit, whereas this hinge is unfolded to form an extended beta-strand, exchange between two CksHs2 subunits. Phosphate and the phosphate analog, metavanadate bind CksHs1 in a shallow pocket and interact with five, conserved residues (Lys11, Arg20, Ser51, Trp54 and Arg71) suggesting a, specific Cks recognition site for a phosphorylated Cdk residue. The, dramatic changes to the Cks fold, assembly and exposed conserved surface, brought about by switching between the bent and extended hinge, conformations are potentially important for the functions of this Cks, homolog and could explain conflicting activities inferred from different, types of genetic experiments.
About this StructureAbout this Structure
1DKS is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain., Arvai AS, Bourne Y, Hickey MJ, Tainer JA, J Mol Biol. 1995 Jun 23;249(5):835-42. PMID:7791211
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