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Src homology 2 (SH2) domains are thought to mediate protein/protein interactions through their ability to bind phosphotyrosine (pY)-containing proteins . They are found in a variety of intracellular signaling molecules important for signal transduction. A sequence alignment of several SH2 domains reveals five highly conserved motifs separated by a less conserved section. It is likely that sequence differences dictate specificity of binding to different tyrosine-phosphorylated ligands. A variety of mechanisms have been proposed for SH2-mediated regulation of signal transduction. SH2 domains may recruit substrates to catalytic domains of the proteins in which they reside, act as adapter proteins to promote complex formation, compete with protein-tyrosine-phosphatases to directly regulate the pY content of the cell, and regulate catalytic activity.