title: The three-dimensional structure of the analgesic alpha-conotoxin, RgIA.
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.
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Clark
authors.forename: Norelle L
authors.initials: NL
authors.lastname: Daly
authors.forename: Reena
authors.initials: R
authors.lastname: Halai
authors.forename: Simon T
authors.initials: ST
authors.lastname: Nevin
authors.forename: David J
authors.initials: DJ
authors.lastname: Adams
authors.forename: David J
authors.initials: DJ
authors.lastname: Craik
mesh_terms: D000595:Amino Acid Sequence; D000700:Analgesics / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D020916:Conotoxins / Q000737:chemistry* / Q000378:metabolism; D052078:Conus Snail / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D017510:Protein Folding
chemical_list: D000700:Analgesics; D020916:Conotoxins; C510079:conotoxin alpha-RgIA, Conus regius