1zp2
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(New page: 200px<br /><applet load="1zp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zp2, resolution 3.0Å" /> '''Structure of the Medi...)
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Revision as of 05:27, 21 November 2007
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Structure of the Mediator subunit cyclin C
Overview
Cyclin C binds the cyclin-dependent kinases CDK8 and CDK3, which regulate, mRNA transcription and the cell cycle, respectively. The crystal structure, of cyclin C reveals two canonical five-helix repeats and a specific, N-terminal helix. In contrast to other cyclins, the N-terminal helix is, short, mobile, and in an exposed position that allows for interactions, with proteins other than the CDKs. A model of the CDK8/cyclin C pair, reveals two regions in the interface with apparently distinct roles. A, conserved region explains promiscuous binding of cyclin C to CDK8 and, CDK3, and a non-conserved region may be responsible for discrimination of, CDK8 against other CDKs involved in transcription. A conserved and cyclin, C-specific surface groove may recruit substrates near the CDK8 active, site. Activation of CDKs generally involves phosphorylation of a loop at a, threonine residue. In CDK8, this loop is longer and the threonine is, absent, suggesting an alternative mechanism of activation that we discuss, based on a CDK8-cyclin C model.
About this Structure
1ZP2 is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Structure of the mediator subunit cyclin C and its implications for CDK8 function., Hoeppner S, Baumli S, Cramer P, J Mol Biol. 2005 Jul 29;350(5):833-42. PMID:15979093
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