1h3h
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STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3 DOMAIN
OverviewOverview
The SH3 domain, which normally recognizes proline-rich sequences, has the potential to bind motifs with an RxxK consensus. To explore this novel specificity, we have determined the solution structure of the Gads T cell adaptor C-terminal SH3 domain in complex with an RSTK-containing peptide, representing its physiological binding site on the SLP-76 docking protein. The SLP-76 peptide engages four distinct binding pockets on the surface of the Gads SH3 domain and upon binding adopts a unique structure characterized by a right-handed 3(10) helix at the RSTK locus, in contrast to the left-handed polyproline type II helix formed by canonical proline-rich SH3 ligands. The structure, and supporting mutagenesis and peptide binding data, reveal a novel mode of ligand recognition by SH3 domains.
About this StructureAbout this Structure
1H3H is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition., Liu Q, Berry D, Nash P, Pawson T, McGlade CJ, Li SS, Mol Cell. 2003 Feb;11(2):471-81. PMID:12620234
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