1PDR

CRYSTAL STRUCTURE OF THE THIRD PDZ DOMAIN FROM THE HUMAN HOMOLOG OF DISCS LARGE PROTEIN

Summary for 1PDR

• Entry DOI: 10.2210/pdb1pdr/pdb
• Descriptor: HUMAN DISCS LARGE PROTEIN (2 entities in total)
• Functional Keywords: signal transduction, sh3 domain
• Biological source: Homo sapiens (human)
• Cellular location: Membrane ; Peripheral membrane protein : Q12959
• Total number of polymer chains: 1
• Total formula weight: 10556.71

Authors

Cabral, J.M.,Liddington, R. (deposition date: 1996-07-26, release date: 1997-07-23, Last modification date: 2024-02-14)

Primary citation

Morais Cabral, J.H.,Petosa, C.,Sutcliffe, M.J.,Raza, S.,Byron, O.,Poy, F.,Marfatia, S.M.,Chishti, A.H.,Liddington, R.C.
Crystal structure of a PDZ domain.
Nature, 382:649-652, 1996

PubMed 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.

PubMed: 8757139
DOI: 10.1038/382649a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)