Crystal structure of a PDZ domain

Nature. 1996 Aug 15;382(6592):649-52. doi: 10.1038/382649a0.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Crystallography, X-Ray
  • Drosophila
  • Genes, Tumor Suppressor
  • Humans
  • Membrane Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Proteins / chemistry*
  • Proteins / genetics
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid

Substances

  • Adaptor Proteins, Signal Transducing
  • DLG1 protein, human
  • Membrane Proteins
  • Proteins
  • Recombinant Proteins