The three-dimensional structure of the analgesic alpha-conotoxin, RgIA

FEBS Lett. 2008 Mar 5;582(5):597-602. doi: 10.1016/j.febslet.2008.01.027. Epub 2008 Jan 31.

Abstract

The alpha-conotoxin RgIA is a selective antagonist of the alpha9alpha10 nicotinic acetylcholine receptor and has been shown to be a potent analgesic and reduces nerve injury associated inflammation. RgIA was chemically synthesized and found to fold into two disulfide isomers, globular and ribbon. The native globular isomer inhibited ACh-evoked currents reversibly in oocytes expressing rat alpha9alpha10 nAChRs but the ribbon isomer was inactive. We determined the three-dimensional structure of RgIA using NMR methods to assist in elucidating the molecular role of RgIA in analgesia and inflammation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Analgesics / chemistry*
  • Analgesics / metabolism
  • Animals
  • Conotoxins / chemistry*
  • Conotoxins / metabolism
  • Conus Snail / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Oxidation-Reduction
  • Protein Folding

Substances

  • Analgesics
  • Conotoxins
  • conotoxin alpha-RgIA, Conus regius