An overview of Src inhibitor
Src tyrosine kinase is composed of c-terminal to n-terminal, including four basic structural domains, namely SH1 (Src Homology 1), SH2, SH3 and SH4, in which SH1 is highly homologous to the first-order structure of Src family catalytic domain. Most Src family proteins have an autonomous phosphorylation site equivalent to Tyr527 at SH1.SH2 is composed of protein components with a length of about 100 amino acid residues, which is relatively conservative and mainly mediates the interconnection of various signal proteins in the cytoplasm to form protein heteropolymer complex, thus regulating signal transmission. SH3 is a conserved amino acid sequence with about 50 amino acid residues. Current studies have found that the recognition site of SH3 is the proline rich region PXXP, which can bind to the target protein through proline with hydrophobic amino terminal residues. SH3 plays a role in subcellular localization and cytoskeletal protein interactions. SH4 is a unique structural domain that connects a saturated 14-alkyl fatty acid.