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1b07
From Proteopedia
| 1b07, resolution 2.50Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1b07 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
See Also
Reference
- Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA. Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors. Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931
