Src homology 3 (SH3) domains are involved in the regulation of important cellular pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of polyproline and a number of noncanonical sequences by SH3 domains has been extensively studied by crystallography, nuclear magnetic resonance and other methods.

Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.

SH3 domains mediate many important protein–protein interactions. The molecular basis of the binding of these domains to their ligands has been revealed, making it possible to identify SH3-binding sites in new proteins. Src homology 3 (SH3) domains have recently emerged as the darlings of the structural biology set.

2017年10月3日 · SH3 domains are protein modules that mediate protein-protein interactions in many eukaryotic signal transduction pathways. The majority of SH3 domains studied thus far act by binding to proline-rich sequences in partner proteins, but a growing number of studies have revealed alternative recognition mechanisms.

2021年3月12日 · We show that the identity of the host protein and the position of the SH3 domains within their host are critical for PPI specificity, for cellular functions and for key biophysical processes such...

SH3 domains are ubiquitous intracellular protein modules; structural and functional studies are revealing how they interact with their proline-rich ligands to promote the formation of specific protein aggregates.

SH3 domains are about 60–70 residues long and are found in a large number of proteins involved in different cellular processes such as intracellular signaling, protein trafficking, cytoskeletal organization, and immune response. The SH3 domain family is one of the most populated family in many proteomes, from yeast to man.

4 天之前 · A scientific resource for the SH3 protein domain containing information on structure, function, and domain binding to proline-rich motifs.

1994年1月1日 · 1. The SH3 Fold The basic fold of the SH3 domain consists of an antiparallel five or six stranded fl-sandwich. The two fl-sheets pack against each other at approximately a right angle (Fig. 2). The domain has a globular shape with a diameter of about 30 A. The N- and C-termini are close in space, as expected for a structurally independent module.

2012年6月20日 · The structure of the SH3 domain in isolated state and surrounded by protein, ligand conformation and specificity of the peptide-binding pocket of SH3 have been extensively studied by crystallography and NMR.