Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR036034
PDZ domains (also known as Discs-large homologous regions (DHR) or GLGF)) are found in diverse signalling proteins in bacteria, yeasts, plants, insects and vertebrates
[2, 1]. PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences
[1]. In most cases, interaction between a PDZ domain and its target is constitutive, with a binding affinity of 1 to 10 microns. However, agonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane, a compartment where high concentrations of phosphatidylinositol 4,5-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin, CASK, Tiam-1) has been demonstrated.
References Imported from IPR036034
1.PDZ domains: targeting signalling molecules to sub-membranous sites. Ponting CP, Phillips C, Davies KE, Blake DJ. Bioessays 19, 469-79, (1997). View articlePMID: 9204764
2.Evidence for PDZ domains in bacteria, yeast, and plants. Ponting CP. Protein Sci. 6, 464-8, (1997). View articlePMID: 9041651
Further reading
3. PDZ domains and their binding partners: structure, specificity, and modification. Lee HJ, Zheng JJ. Cell Commun. Signal 8, 8, (2010). PMID: 20509869