Anolis carolinensis (pS/pT)/PDZ
※ PDZ family introduction The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. The PDZ domain of RGS3 were found to bind to the Tyr304 phosphopeptide of ephrin B2 in recent study (1). Reference
1. Su, Z. (2011) Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein. Eur J Biochem, 271, 1725-36. PMID: 15096211
There are 111 genes. Reviewed (0)
or Unreviewed (111) 
※ PDZ family introduction The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. The PDZ domain of RGS3 were found to bind to the Tyr304 phosphopeptide of ephrin B2 in recent study (1). Reference
1. Su, Z. (2011) Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein. Eur J Biochem, 271, 1725-36. PMID: 15096211
There are 111 genes. Reviewed (0)
or Unreviewed (111)