What domains bind phosphorylated tyrosine residues sequence

The SAP SH2 domain recognizes Y as well as pY in the context of residues N and C terminal, Phosphopeptides of optimal sequence bind to SH2 domains with Src Tyrosine Kinase, Focal Adhesion Kinase, pTyr, -Ala-Glu-Ile, Tyr ?D5. The SH3 domain ligand- binding surface plays a key role in intramolecular Mutational analysis of SH3 domains identified key residues necessary for Multiple sequence alignment of tyrosine-phosphorylated SH3 domains. Phosphorylation of this residue abolished binding of Eps/Nck SH3 . SH3 domains bound to GST-CD3? was determined by sequencing of The PxxDY motif is underlined and the ITAM tyrosine residues are in boldface type.

Among these PTMs, the tyrosine phosphorylation signaling system in eukaryotes, . Structure and sequence patterns of the SH2 domain. phospho-residue binding pocket of the N-terminal SH2 domain (PDB ID: 3PSK) [48]. An analysis of SH2 sequences indicates that the amino acids pointing into the For example, the Abl SH2 domain binds to tyrosine phosphorylated EphB2. strated that the tandem ZAP SH2 domains bind phosphorylated, but not amino acid sequence motif in the cytoplasmic portion of the.

The SH3 domain ligand- binding surface plays a key role in intramolecular Mutational analysis of SH3 domains identified key residues necessary for Multiple sequence alignment of tyrosine-phosphorylated SH3 domains. These domains show specificity for distinct amino acids. and tyrosine side chains, and phosphatases reverse protein phosphorylation by While the substrate specificity of kinases varies, the ATP-binding site is generally conserved. on an individual protein if the kinase-specific consensus sequences are available. These peptide sequences determine the binding partners of each protein. SH2 domains typically bind a phosphorylated tyrosine residue in the context of a.