David Auble
SH3 domains are compact structures that bind short proline-rich sequences. The SH3 domain is a barrel-shaped structure composed of antiparallel β-strands. The β-strands form two sheets that are nearly perpendicular to each other. The proline-rich peptide binding site is located in a cleft on one side of the barrel, and the peptide adopts an unusual helical conformation with three residues per turn. Interactions between SH3 domains and proline-rich peptides are mainly hydrophobic and typically rather weak. SH3 domains are often found in proteins with other protein-protein interaction motifs (such as SH2 domains) where they are thought to augment the affinity for interaction partners. Structures of many SH3 domains have been solved; the images here are derived from 1aze.
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