Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M400548200
DC FieldValue
dc.titleComparison of Taurine- and Glycine-induced Conformational Changes in the M2-M3 Domain of the Glycine Receptor
dc.contributor.authorHan, N.-L.R.
dc.contributor.authorClements, J.D.
dc.contributor.authorLynch, J.W.
dc.date.accessioned2014-10-27T08:24:21Z
dc.date.available2014-10-27T08:24:21Z
dc.date.issued2004-05-07
dc.identifier.citationHan, N.-L.R., Clements, J.D., Lynch, J.W. (2004-05-07). Comparison of Taurine- and Glycine-induced Conformational Changes in the M2-M3 Domain of the Glycine Receptor. Journal of Biological Chemistry 279 (19) : 19559-19565. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M400548200
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100308
dc.description.abstractIn the ionotropic glutamate receptor, the global conformational changes induced by partial agonists are smaller than those induced by full agonists. However, in the pentameric ligand-gated ion channel receptor family, the structural basis of partial agonism is not understood. This study investigated whether full and partial agonists induce different conformation changes in the glycine receptor chloride channel (GlyR). A substituted cysteine accessibility analysis demonstrated previously that glycine binding induced an increase in surface accessibility of all residues from Arg271 to Lys 276 in the M2-M3 domain of the homomeric α1 GlyR. Here we compare the surface accessibility changes induced by the full agonist, glycine, and the partial agonist, taurine. In GlyRs incorporating the A272C, S273C, L274C, or P275C mutation, the reaction rate of the cysteine-specific compound, methanethiosulfonate ethyltrimethylammonium, depended on how strongly the receptors were activated but was agonist-independent. Reaction rates could not be compared in the R271C and K276C mutant GlyRs because methanethiosulfonate ethyltrimethylammonium did not modify the extremely small currents induced by saturating taurine or equivalent low glycine concentrations. The results indicate that bound taurine and glycine molecules impose identical conformational changes to the M2-M3 domain. We therefore conclude that the higher efficacy of glycine is due to an increased ability to stabilize a common activated configuration.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M400548200
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1074/jbc.M400548200
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume279
dc.description.issue19
dc.description.page19559-19565
dc.description.codenJBCHA
dc.identifier.isiut000221164500023
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