2sem: Difference between revisions
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'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR''' | '''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR''' | ||
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[[Category: Turck, C W.]] | [[Category: Turck, C W.]] | ||
[[Category: Zuckermann, R N.]] | [[Category: Zuckermann, R N.]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: | [[Category: Peptoid]] | ||
[[Category: | [[Category: Proline-rich motif]] | ||
[[Category: | [[Category: Protein-protein recognition]] | ||
[[Category: | [[Category: Sh3 domain]] | ||
[[Category: | [[Category: Signal transduction]] | ||
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Revision as of 14:18, 4 May 2008
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. 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 Sun May 4 17:18:00 2008
