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Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2

, : Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2. Structure (London) 2(11): 1029-1040

Background: Growth factor receptor-bound protein 2 (GRB2) is an adaptor protein with three Src homology (SH) domains in the order SH3-SH2-SH3. Both SH3 domains of GRB2 are necessary for interaction with the protein Son of sevenless (Sos), which acts as a Ras activator. Thus, GRB2 mediates signal transduction from growth factor receptors to Ras and is thought to be a key molecule in signal transduction. Results: The three-dimensional structure of the carboxy-terminal SH3 domain of GRB2 (GPB2 C-SH3) was determined by NMR spectroscopy. The SH3 structure consists of six beta-strands arranged in two beta-sheets that are packed together perpendicularly with two additional beta-strands forming the third beta-sheet. GR-B2 C-SH3 is very similar to SH3 domains from other proteins. The binding site of the ligand peptide (VPPPVPPRRR) derived from the Sos protein was mapped on the GPB2 C-SH3 domain indirectly using 1H and 15N chemical shift changes, and directly using several intermolecular nuclear Overhauser effects. Conclusions: Despite the structural similarity among the known SH3 domains, the sequence alignment and the secondary structure assignments differ. We therefore propose a standard description of the SH3 structures to facilitate comparison of individual SH3 domains, based on their three-dimensional structures. The binding site of the ligand peptide on GRB2 C-SH3 is in good agreement with those found in other SH3 domains.


PMID: 7881903

DOI: 10.1016/s0969-2126(94)00106-5

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