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PDBsum entry 1dkt
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Cell division
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PDB id
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1dkt
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the human cell cycle protein ckshs1: single domain fold with similarity to kinase n-Lobe domain.
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Authors
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A.S.Arvai,
Y.Bourne,
M.J.Hickey,
J.A.Tainer.
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Ref.
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J Mol Biol, 1995,
249,
835-842.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystallization and preliminary crystallographic study of human ckshs1: a cell cycle regulatory protein.
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Authors
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A.S.Arvai,
Y.Bourne,
D.Williams,
S.I.Reed,
J.A.Tainer.
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Ref.
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Proteins, 1995,
21,
70-73.
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PubMed id
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