Referenced in: none

Automatically associated channels: Kir2.3

Title: Crystal structure of a PDZ domain.

Authors: J H Morais Cabral, C Petosa, M J Sutcliffe, S Raza, O Byron, F Poy, S M Marfatia, A H Chishti, R C Liddington

Journal, date & volume: Nature, 1996 Aug 15 , 382, 649-52

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/8757139

Abstract
PDZ domains (also known as DHR domains or GLGF repeats) are approximately 90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association. Here we report the crystal structure of the third PDZ domain of the human homologue of the Drosophila discs-large tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel beta-barrel flanked by three alpha-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.