1h3h: Difference between revisions

Revision as of 06:33, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1h3h.png

Template:STRUCTURE 1h3h

STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3 DOMAINSTRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3 DOMAIN

Template:ABSTRACT PUBMED 12620234

About this StructureAbout this Structure

1H3H is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3 DOMAIN'''
+===STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF AN RXXK-CONTAINING SLP-76 PEPTIDE BY THE GADS C-TERMINAL SH3 DOMAIN===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12620234}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12620234 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12620234}}
 ==About this Structure==
-H3H is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3H OCA].
+H3H is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3H OCA].
 ==Reference==
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 [[Category: Sh3 domain]]
 [[Category: T-cell signaling]]
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