1oeb

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[[Image:1oeb.gif|left|200px]]
[[Image:1oeb.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oeb OCA], [http://www.ebi.ac.uk/pdbsum/1oeb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oeb RCSB]</span>
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'''MONA/GADS SH3C DOMAIN'''
'''MONA/GADS SH3C DOMAIN'''
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[[Category: Mouchiroud, G.]]
[[Category: Mouchiroud, G.]]
[[Category: Sondermann, H.]]
[[Category: Sondermann, H.]]
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[[Category: dimer]]
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[[Category: Dimer]]
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[[Category: gad]]
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[[Category: Gad]]
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[[Category: mona]]
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[[Category: Mona]]
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[[Category: sh3]]
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[[Category: Sh3]]
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[[Category: signal tranduction]]
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[[Category: Signal tranduction]]
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[[Category: slp-76]]
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[[Category: Slp-76]]
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Revision as of 00:44, 3 May 2008

Image:1oeb.gif

Template:STRUCTURE 1oeb

MONA/GADS SH3C DOMAIN


Overview

SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key issue in understanding the molecular basis of SH3 domain interactions. The Grb2-like adaptor protein Mona/Gads associates stably with the T-cell receptor signal transducer SLP-76. The crystal structure of a complex between the C-terminal SH3 domain (SH3C) of Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide lacks the canonical SH3 domain binding motif P-x-x-P and does not form a frequently observed poly-proline type II helix. Instead, it adopts a clamp-like shape around the circumfence of the SH3C beta-barrel. The central R-x-x-K motif of the peptide forms a 3(10) helix and inserts into a negatively charged double pocket on the SH3C while several other residues complement binding through hydrophobic interactions, creating a short linear SH3C binding epitope of uniquely high affinity. Interestingly, the SH3C displays ion-dependent dimerization in the crystal and in solution, suggesting a novel mechanism for the regulation of SH3 domain functions.

About this Structure

1OEB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:12773374 Page seeded by OCA on Sat May 3 03:44:09 2008

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