2sem
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(New page: 200px<br /><applet load="2sem" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sem, resolution 2.2Å" /> '''SEM5 SH3 DOMAIN COMPL...)
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Revision as of 11:53, 21 November 2007
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SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR
Overview
Src homology 3 (SH3) and WW protein interaction domains bind specific, proline-rich sequences. However, instead of recognizing critical prolines, on the basis of side chain shape or rigidity, these domains broadly, accepted amide N-substituted residues. Proline is apparently specifically, selected in vivo, despite low complementarity, because it is the only, endogenous N-substituted amino acid. This discriminatory mechanism, explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The, mechanism can be exploited: screening a series of ligands in which key, prolines were replaced by nonnatural N-substituted residues yielded a, ligand that selectively bound the Grb2 SH3 domain with 100 times greater, affinity.
About this Structure
2SEM is a Single protein structure of sequence from Caenorhabditis elegans with ACE as ligand. Full crystallographic information is available from OCA.
Reference
Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors., Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA, Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931
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