1lew

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(New page: 200px<br /> <applet load="1lew" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lew, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:52, 12 November 2007


1lew, resolution 2.3Å

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CRYSTAL STRUCTURE OF MAP KINASE P38 COMPLEXED TO THE DOCKING SITE ON ITS NUCLEAR SUBSTRATE MEF2A

Overview

The structures of the MAP kinase p38 in complex with docking site peptides, containing a phi(A)-X-phi(B) motif, derived from substrate MEF2A and, activating enzyme MKK3b, have been solved. The peptides bind to the same, site in the C-terminal domain of the kinase, which is both outside the, active site and distinct from the "CD" domain previously implicated in, docking site interactions. Mutational analysis on the interaction of p38, with the docking sites supports the crystallographic models and has, uncovered two novel residues on the docking groove that are critical for, binding. The two peptides induce similar large conformational changes, local to the peptide binding groove. The peptides also induce unexpected, and different conformational changes in the active site, as well as, structural disorder in the phosphorylation lip.

About this Structure

1LEW is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b., Chang CI, Xu BE, Akella R, Cobb MH, Goldsmith EJ, Mol Cell. 2002 Jun;9(6):1241-9. PMID:12086621

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