The three-dimensional structure of the analgesic alpha-conotoxin, RgIA |
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Authors: | Clark Richard J Daly Norelle L Halai Reena Nevin Simon T Adams David J Craik David J |
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Affiliation: | Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia. |
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Abstract: | The alpha-conotoxin RgIA is a selective antagonist of the alpha9alpha10 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 alpha9alpha10 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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Keywords: | Conotoxin Nuclear magnetic resonance Analgesic Oxidative folding Disulfide isomers |
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