SH3 domain


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SH3 domain

Src-homology 3 domain. A small, circa-60-amino acid domain which binds to proline-rich peptides. Proteins with SH3 domain include CDC24, CDC25, crk adaptor protein, cytoplasmic tyrosine kinases—e.g., abl, src, phospholipase, PI3 kinase, Ras GTPase activating protein.
References in periodicals archive ?
Rubin et al [16] identified two major genes correlated to chicken domestication process through selective-sweep analysis of chicken genome; thyroid stimulating hormone receptor (TSHR) and SH3 domain containing ring finger 2 (SH3RF2) gene.
SH3RF2, SH3 domain containing ring finger 2; KO, knockout; QM7, quail myoblast.
These sequences are separated from the PQVPLR binding site, and would hardly interact with SH3 domain, but instead with a different region of SH3 domain containing protein (45).
C-terminal portion of p22-phox contains PRR domain (proline-rich region) ((47), which is capable to interact with SH3 domains in p47-phox, this interaction critical to both membrane recruitment of p47-phox and oxidase activation.
Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognition of a polyproline type II helix and an adjacent alpha-helix of p22phox.
SAM and SH3 domain containing protein 1 (SASH1) is identified to be a tumor suppressor gene for breast cancer.
The central region of p104 contains three proline-rich (PXXP) motifs that are known to interact with the SH3 domain. Since CrkII contains an SH2 and two SH3 domains, it was investigated whether p104 directly interacts with CrkII through its PXXP motifs.
Crk was originally isolated as the oncogene fusion product of the CT10 chicken retrovirus [35] and the CrkII protein contains an aminoterminal SH2 domain and two SH3 domains [36].
Because a GST fusion protein containing an SH2 domain of Fyn can bind to PECAM-1 but an SH3 domain of Fyn cannot, the SH2 domain of cSrc appears to be involved in c-Src binding to tyrosine-phosphorylated PECAM-1.
Baker and his colleagues focused on a 57-unit chain, containing 18 different amino, acids, from a protein subunit called the SH3 domain. This sequence is found in many large proteins that act as chemical messengers within and between cells.
The researchers screened the candidate structures for the ability to bind to a peptide that attaches at a specific binding site within the SH3 domain. They did not try to replace the amino acids forming the binding site, Baker says.