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1b07

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{{STRUCTURE_1b07| PDB=1b07 | SCENE= }}
{{STRUCTURE_1b07| PDB=1b07 | SCENE= }}
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'''CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''
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===CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR===
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==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 Jun 30 17:57:51 2008''

Revision as of 14:57, 30 June 2008

Image:1b07.png

Template:STRUCTURE 1b07

CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

Template:ABSTRACT PUBMED 9851931

About this Structure

1B07 is a Single protein structure of sequence from Mus musculus. 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 Mon Jun 30 17:57:51 2008

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