Click on the picture for a stereo one.



SH3 domain is a small conserved sequence of about 60 amino acid residues that interacts with proline-rich peptides to form protein aggregates. Structurally, the SH3 domain folds as a compact beta-barrel of five anti-parallel beta-strands which bring the amino and the carboxyl termini of the domain close to each other. The ligands of the SH3 domains are ten amino acid residue peptides that form a left- handed polyproline (PPII) helix. Functionally, the SH3 domain is involved in cell-cell communication and signal transduction from the cell surface to the nucleus. It acts as part of an adapter molecule and recruits downstream proteins in a signalling pathway.
If interested, you can read more information about the different parts of the domain by clicking on those parts on the SH3 Walk-Through.



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By Fariba Fana
September 8, 1997