Clark, Richard J., Daly, Norelle L., Halai, Reena, Nevin, Simon T., Adams, David J., and Craik, David J. (2008) The three-dimensional structure of the analgesic α-conotoxin, RgIA. FEBS Letters, 582 (5). pp. 597-602.

PDF (Published Version) - Published Version Restricted to Repository staff only

32

Abstract

The α-conotoxin RgIA is a selective antagonist of the α9α10 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 α9α10 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.

Actions (Repository Staff Only)

Item Control Page