Title

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

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.

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Link to publisher version (DOI)

http://dx.doi.org/10.1016/j.febslet.2008.01.027