1OEB

Mona/Gads SH3C domain

Summary for 1OEB

• Entry DOI: 10.2210/pdb1oeb/pdb
• Related: 1H3H
• Descriptor: GRB2-RELATED ADAPTOR PROTEIN 2, LYMPHOCYTE CYTOSOLIC PROTEIN 2, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: protein binding, sh3 domain-complex, sh3, slp-76, dimer, mona, gads, signal tranduction
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Cytoplasm (Probable): Q60787
• Total number of polymer chains: 4
• Total formula weight: 17051.53

Authors

Harkiolaki, M.,Lewitzky, M.,Gilbert, R.J.C.,Jones, E.Y.,Bourette, R.P.,Mouchiroud, G.,Sondermann, H.,Moarefi, I.,Feller, S.M. (deposition date: 2003-03-24, release date: 2003-04-02, Last modification date: 2024-05-08)

Primary citation

Harkiolaki, M.,Lewitzky, M.,Gilbert, R.J.C.,Jones, E.Y.,Bourette, R.P.,Mouchiroud, G.,Sondermann, H.,Moarefi, I.,Feller, S.M.
Structural Basis for SH3 Domain-Mediated High-Affinity Binding between Mona/Gads and Slp-76
Embo J., 22:2571-, 2003

PubMed Abstract: 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.

PubMed: 12773374
DOI: 10.1093/EMBOJ/CDG258

Experimental method

X-RAY DIFFRACTION (1.76 Å)