1b07: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b07 OCA], [http://www.ebi.ac.uk/pdbsum/1b07 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b07 RCSB]</span>
}}
}}


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[[Category: Turck, C W.]]
[[Category: Turck, C W.]]
[[Category: Zuckermann, R N.]]
[[Category: Zuckermann, R N.]]
[[Category: PYL]]
[[Category: inhibitor]]
[[Category: inhibitor]]
[[Category: peptoid]]
[[Category: peptoid]]
Line 35: Line 37:
[[Category: signal transduction]]
[[Category: signal transduction]]


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Revision as of 15:50, 30 March 2008

File:1b07.gif


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1b07, resolution 2.50Å
Ligands: PYL
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRK 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

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

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