| Literature DB >> 18242183 |
Richard J Clark1, Norelle L Daly, Reena Halai, Simon T Nevin, David J Adams, David J Craik.
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.Entities:
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Year: 2008 PMID： 18242183 DOI： 10.1016/j.febslet.2008.01.027
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124