1H, 13C and 15N resonance assignments of the PDZ of microtubule-associated serine/threonine kinase 205 (MAST205) in complex with the C-terminal motif from the rabies virus glycoprotein

Biomol NMR Assign. 2009 Jun;3(1):45-8. doi: 10.1007/s12104-008-9138-0. Epub 2009 Jan 13.

Abstract

Most of microbes hijack the cellular machinery to their advantage by interacting with specific target of the host cell. Glycoprotein of rabies virus is a key factor controlling the homeostasis of infected neuronal cells and proteins belonging to the human microtubule associated serine threonine kinase family have been identified as potential cellular partners. As a first step towards its structural study, we have assigned the backbone and side chain nuclei resonances of the PDZ domain (PSD-95, Discs Large, ZO-1) of MAST205 in complex with the C-terminal residues of the glycoprotein of rabies virus. The BMRB accession code is 155972.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Carbon Isotopes / chemistry
  • Glycoproteins / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Microtubule-Associated Proteins / chemistry*
  • Molecular Sequence Data
  • Multiprotein Complexes / chemistry
  • Nitrogen Isotopes / chemistry
  • Protein Binding
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Structure, Tertiary
  • Protons
  • Rabies virus / chemistry*
  • Viral Proteins / chemistry*

Substances

  • Carbon Isotopes
  • Glycoproteins
  • Microtubule-Associated Proteins
  • Mtssk protein, mouse
  • Multiprotein Complexes
  • Nitrogen Isotopes
  • Protons
  • Viral Proteins
  • Protein Serine-Threonine Kinases