Unravelling the conformational plasticity of the extracellular domain of a prokaryotic nAChR homologue in solution by NMR

Biochemistry. 2011 Nov 15;50(45):9681-3. doi: 10.1021/bi201223u. Epub 2011 Oct 20.

Abstract

Pentameric ligand-gated ion channels (pLGICs) of the Cys loop family are transmembrane glycoproteins implicated in a variety of biological functions. Here, we present a solution NMR study of the extracellular domain of a prokaryotic pLGIC homologue from the bacterium Gloeobacter violaceus that is found to be a monomer in solution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Cyanobacteria / chemistry*
  • Cyanobacteria / genetics
  • Cysteine Loop Ligand-Gated Ion Channel Receptors / chemistry*
  • Cysteine Loop Ligand-Gated Ion Channel Receptors / genetics
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Subunits
  • Receptors, Nicotinic / chemistry*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Solutions
  • Structural Homology, Protein

Substances

  • Bacterial Proteins
  • Cysteine Loop Ligand-Gated Ion Channel Receptors
  • Protein Subunits
  • Receptors, Nicotinic
  • Recombinant Proteins
  • Solutions