Crystal structure of a PDZ domain

Cabral, J. H. M., Petosa, C., Sutcliffe, M. J., Raza, S., Byron, O. , Poy, F., Marfatia, S. M., Chishti, A. H. and Liddington, R. C. (1996) Crystal structure of a PDZ domain. Nature, 382(6592), pp. 649-652. (doi: 10.1038/382649a0) (PMID:8757139)

Abstract

PDZ domains (also known as DHR domains or GLGF repeats) are ˜90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes1. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity2–4. 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 association5. 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 β-barrel flanked by three α-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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Byron, Professor Olwyn
• Authors: Cabral, J. H. M., Petosa, C., Sutcliffe, M. J., Raza, S., Byron, O., Poy, F., Marfatia, S. M., Chishti, A. H., and Liddington, R. C.
• College/School: College of Medical Veterinary and Life Sciences > School of Life Sciences
• Journal Name: Nature
• Publisher: Nature Publishing Group
• ISSN: 0028-0836
• ISSN (Online): 1476-4687