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.

Here we investigate the changes in residue-specific 15 N relaxation rates in Sem-5 C-SH3 domain on ligand binding. We correlate these changes with the observed cooperativity of the binding process.

2018年12月21日 · The SH3 domain mediates protein–protein interactions with target proteins and putatively binds peptides containing a PXXP motif (18), whereas the SH2 domain binds primarily to phosphorylated tyrosines.

2012年8月14日 · Here we discuss the structural basis of non-consensus SH3 ligand binding and the dominant role of the SH3 domain specificity zone in selective target recognition, and review some of the best-characterized examples of such interactions.

The SRC Homology 3 Domain (or SH3 domain) is a small protein domain of about 60 amino acid residues. Initially, SH3 was described as a conserved sequence in the viral adaptor protein v-Crk. This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src .

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.

2022年9月1日 · SRC homology (SH)3 domains mediate intramolecular associations and form supramodules with their own supertertiary structures, which regulate their host protein functions. Protein interactions mediated by SH3 modules are highly dependent on …

结合 mSOS 肽（红色）的 SEM-5 的羧基末端 SH3 结构域。 S rc- 同源 3 (SH3) 结构域结合脯氨酸富集肽，这种肽会与最小的共有 Pro-X-X-Pro 形成左侧聚脯氨酸 II 型螺旋。 脂肪族残基通常在每个脯氨酸的前面，每个脂肪族脯氨酸对则与 SH3 结构域上的疏水口袋相结合。 原则上，配体能以任意一种方向结合。 其它非脯氨酸残基（经常是 Arg）结合 SH3 结构域，并形成结合核心的一部分。 这类肽通常结合 SH3 结构域，µM 范围为 K d。 SH3 结构域上涉及环的三次相互作用会使 …

2008年7月1日 · In addition, we show that the C-terminal SH3 domain binding to a polyproline region N-terminal to the DH domain of the Tim subgroup of Dbl-family proteins provides a unique mechanism of regulated autoinhibition of exchange activity that is functionally linked to the interactions between the autoinhibitory helix and the DH domain.

4 天之前 · The C-terminal SH3 domain of SEM-5 bound to mSOS peptide (red). Src-homology 3 (SH3) domains bind to Pro-rich peptides that form a left-handed poly-Pro type II helix, with the minimal consensus Pro-X-X-Pro. An aliphatic residue usually precedes each proline, with each of the aliphatic-Pro pairs binding to a hydrophobic pocket on the SH3 domain.