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The three‐dimensional structure of the analgesic α‐conotoxin, RgIA
Author(s) -
Clark Richard J.,
Daly Norelle L.,
Halai Reena,
Nevin Simon T.,
Adams David J.,
Craik David J.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.01.027
Subject(s) - conotoxin , chemistry , analgesic , antagonist , acetylcholine receptor , nicotinic acetylcholine receptor , pharmacology , nicotinic agonist , acetylcholine , disulfide bond , biophysics , stereochemistry , receptor , biochemistry , medicine , venom , biology
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.