1b38: Difference between revisions

Revision as of 18:08, 30 June 2008

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File:1b38.png

Template:STRUCTURE 1b38

HUMAN CYCLIN-DEPENDENT KINASE 2HUMAN CYCLIN-DEPENDENT KINASE 2

Template:ABSTRACT PUBMED 10085115

About this StructureAbout this Structure

1B38 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity., Brown NR, Noble ME, Lawrie AM, Morris MC, Tunnah P, Divita G, Johnson LN, Endicott JA, J Biol Chem. 1999 Mar 26;274(13):8746-56. PMID:10085115

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OCA

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 {{STRUCTURE_1b38|  PDB=1b38  |  SCENE=  }}
-'''HUMAN CYCLIN-DEPENDENT KINASE 2'''
+===HUMAN CYCLIN-DEPENDENT KINASE 2===
-==Overview==
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-We have prepared phosphorylated cyclin-dependent protein kinase 2 (CDK2) for crystallization using the CDK-activating kinase 1 (CAK1) from Saccharomyces cerevisiae and have grown crystals using microseeding techniques. Phosphorylation of monomeric human CDK2 by CAK1 is more efficient than phosphorylation of the binary CDK2-cyclin A complex. Phosphorylated CDK2 exhibits histone H1 kinase activity corresponding to approximately 0.3% of that observed with the fully activated phosphorylated CDK2-cyclin A complex. Fluorescence measurements have shown that Thr160 phosphorylation increases the affinity of CDK2 for both histone substrate and ATP and decreases its affinity for ADP. By contrast, phosphorylation of CDK2 has a negligible effect on the affinity for cyclin A. The crystal structures of the ATP-bound forms of phosphorylated CDK2 and unphosphorylated CDK2 have been solved at 2.1-A resolution. The structures are similar, with the major difference occurring in the activation segment, which is disordered in phosphorylated CDK2. The greater mobility of the activation segment in phosphorylated CDK2 and the absence of spontaneous crystallization suggest that phosphorylated CDK2 may adopt several different mobile states. The majority of these states are likely to correspond to inactive conformations, but a small fraction of phosphorylated CDK2 may be in an active conformation and hence explain the basal activity observed.
+The line below this paragraph, {{ABSTRACT_PUBMED_10085115}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10085115}}
 ==About this Structure==
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 [[Category: Serine/threonine protein kinase]]
 [[Category: Transferase]]
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