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

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.

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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.

Item ID: 27102
Item Type: Article (Research - C1)
ISSN: 1873-3468
Date Deposited: 11 Jun 2013 06:10
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060112 Structural Biology (incl Macromolecular Modelling) @ 100%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
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