What does a SH2 domain do?
Src homology 2 (SH2) domains are protein modules (of approximately 100 amino acids) found in many proteins involved in tyrosine kinase signalling cascades. Their function is to bind tyrosine-phosphorylated sequences in specific protein targets.
What is GRB2 and SOS?
Grb2 protein, which is the downstream effector of the EGF receptor, acts as an adaptor protein between the EGF receptor and the Ras guanine-nucleotide exchange factor, son of sevenless (Sos) protein. Sos protein regulates the action of Ras protein by promoting the exchange of GDP for GTP.
What do SH3 domains recognize?
SH3 domains have been identified as protein modules that recognize proline-rich sequences (Mayer et al. 1988; Kaneko et al. 2008). The peptide sequence qPxqP, which binds to the SH3 domain, can be represented as two qP dipeptides linked by any residue x where q is a hydrophobic residue (Kay et al.
Where are the SH2 domains located in a protein?
SH2 domain. The SH2 ( S rc H omology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins.
Where are the SH2 domains located in PDBsum?
PDBsum. structure summary. The SH2 ( S rc H omology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins.
What is the SH2 domain of Src homology 2?
The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps [PMID: 3025655]. Similar sequences were later found in many other intracellular signal-transducing proteins [PMID: 1377638].
How does SH2 domain discriminate its targets?
These studies have pointed out that SH2 domains discriminate their targets by making important contacts with residues from position +1 up to +4 in the ligand peptide. For example, the SH2 domain of the FES, MST, SYK, RASA1, and BRDG1 proteins prefers the pYExxx, pYDxxx, pYxxLx, pYxxPx, or pYxxxP respectively ( Figure 4 ).