3sem
From Proteopedia
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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
3SEM is a Single protein structure of sequence from Caenorhabditis elegans. 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
Page seeded by OCA on Tue Nov 20 19:58:27 2007
