The SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein [2] and in many other intracellular signal-transducing proteins. [3] SH2 domains bind to phosphorylated tyrosine residues on other proteins, modifying the function or activity of the SH2-containing protein.

SH2 (Src Homology 2) domains are among the best characterized and most studied protein-protein interaction (PPIs) modules able to bind and recognize sequences presenting a phosphorylated tyrosine. This post-translational modification is a key ...

The SH2 domain is a key regulator of allosteric kinase regulation and may play a role in both the inactive as well as the active states of tyrosine kinases. It is therefore no surprise that mutations have been identified in patients that compromise SH2 function and as a …

SH2 domains recognize both permissive and non-permissive residues in prospective phosphopeptide ligands that together contribute to greater selectivity than is predicted from positive factors alone.

Feb 15, 2024 · Structure-guided drug design has enabled the discovery of a cell-permeable covalent inhibitor of the SOCS2 SH2 domain, a key regulator of cytokine signaling pathways.

5 days ago · Src-homology 2 (SH2) domains are modules of approximately 100 amino acids that bind to specific phospho (pY)-containing peptide motifs. Conventional SH2 domains have a conserved pocket that recognizes pY, and a more variable pocket that binds 3-6 residues C-terminal to the pY to confer specificity.

SH2 domains bind proteins carrying phospho-tyrosines and therefore offer a mechanism for protein to sense changes caused by signals that modulate phosphorylation of tyrosines.

Feb 14, 2005 · The Src homology 2 (SH2) domain is the most prevalent protein binding module that recognizes phosphotyrosine. This approximately 100-amino-acid domain is highly conserved structurally despite being found in a wide variety proteins.

Jan 30, 2004 · This review recapitulates the roles that SH2 domains play in normal and diseased states, describes the successes of SH2 domain research in deciphering their mechanism of action, and provides an overview of the use of SH2 domains as structural templates for the design of inhibitor drugs.

Dec 15, 2022 · In this review, we recapitulate the current knowledge about the structural, folding stability, and binding properties of SH2 domains and their roles in molecular pathways and pathogenesis. Moreover, we focus attention on the different strategies employed to modulate/inhibit SH2 domains binding.