1oeb

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spinqualitylabelsall models 1oeb, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with CD as ligand. Known structural/functional Site: . 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

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