1h3h: Difference between revisions

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[[Image:1h3h.jpg|left|200px]]
{{Seed}}
[[Image:1h3h.png|left|200px]]


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{{STRUCTURE_1h3h|  PDB=1h3h  |  SCENE=  }}  
{{STRUCTURE_1h3h|  PDB=1h3h  |  SCENE=  }}  


'''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==
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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.
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{{ABSTRACT_PUBMED_12620234}}


==About this Structure==
==About this Structure==
1H3H 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].  
1H3H 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==
==Reference==
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[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
[[Category: T-cell signaling]]
[[Category: T-cell signaling]]
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