SH2 domain binding

Definition

Target type: molecularfunction

Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class. [GOC:go_curators, Pfam:PF00017]

SH2 domains are protein modules that specifically recognize and bind to phosphorylated tyrosine residues within target proteins. This interaction is crucial for a wide range of cellular processes, including signal transduction, protein-protein interactions, and regulation of enzyme activity. SH2 domains typically consist of about 100 amino acids and adopt a compact globular structure. They contain a conserved binding pocket that accommodates the phosphorylated tyrosine residue and surrounding amino acid residues. The specificity of SH2 domain binding is determined by the sequence and conformation of the binding site, which allows them to discriminate between different phosphorylated tyrosine residues. Once bound to a phosphorylated target, SH2 domains can recruit other proteins or enzymes, leading to the activation or inhibition of signaling pathways. The binding event can also induce conformational changes in the target protein, modulating its activity or stability. In essence, SH2 domains act as molecular switches that regulate cellular processes by recognizing and binding to specific phosphorylated tyrosine residues. This binding event can initiate signaling cascades, modulate protein-protein interactions, and control the activity of enzymes.'
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Proteins (12)

Compounds (533)