2sem: Difference between revisions

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[[Image:2sem.jpg|left|200px]]
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[[Image:2sem.png|left|200px]]


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{{STRUCTURE_2sem|  PDB=2sem  |  SCENE=  }}  
{{STRUCTURE_2sem|  PDB=2sem  |  SCENE=  }}  


'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''
===SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9851931}}


==About this Structure==
==About this Structure==
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[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:21:24 2008''

Revision as of 08:21, 28 July 2008

File:2sem.png

Template:STRUCTURE 2sem

SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

Template:ABSTRACT PUBMED 9851931

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

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