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

Authors

Richard J. Clark, University of Queensland
Norelle L. Daly, University of Queensland
Reena Halai, University of Queensland
Simon T. Nevin, University of Queensland
David J. Adams, University of QueenslandFollow
David J. Craik, University of Queensland

RIS ID

105647

Publication Details

Clark, R. J., Daly, N. L., Halai, R., Nevin, S. T., Adams, D. J. & Craik, D. J. (2008). The three-dimensional structure of the analgesic α-conotoxin, RgIA. FEBS Letters, 582 (5), 597-602.

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.