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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Paas, Yoav Gortler, Revital Degani-katzav, Nurit Gorodetzki, Lilach |
| Description | Author Affiliation: Degani-Katzav N ( Laboratory of Ion Channels, The Mina and Everard Goodman Faculty of Life Sciences and The Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat Gan 52900, Israel.); Gortler R ( Laboratory of Ion Channels, The Mina and Everard Goodman Faculty of Life Sciences and The Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat Gan 52900, Israel.); Gorodetzki L ( Laboratory of Ion Channels, The Mina and Everard Goodman Faculty of Life Sciences and The Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat Gan 52900, Israel.); Paas Y ( Laboratory of Ion Channels, The Mina and Everard Goodman Faculty of Life Sciences and The Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat Gan 52900, Israel yoav.paas@biu.ac.il.); |
| Abstract | The invertebrate glutamate-gated chloride-selective receptors (GluClRs) are ion channels serving as targets for ivermectin (IVM), a broad-spectrum anthelmintic drug used to treat human parasitic diseases like river blindness and lymphatic filariasis. The native GluClR is a heteropentamer consisting of and ß subunit types, with yet unknown subunit stoichiometry and arrangement. Based on the recent crystal structure of a homomeric GluCl R, we introduced mutations at the intersubunit interfaces where Glu (the neurotransmitter) binds. By electrophysiological characterization of these mutants, we found heteromeric assemblies with two equivalent Glu-binding sites at ß/ intersubunit interfaces, where the GluClß and GluCl subunits, respectively, contribute the 'principal' and 'complementary' components of the putative Glu-binding pockets. We identified a mutation in the IVM-binding site (far away from the Glu-binding sites), which significantly increased the sensitivity of the heteromeric mutant receptor to both Glu and IVM, and improved the receptor subunits' cooperativity. We further characterized this heteromeric GluClR mutant as a receptor having a third Glu-binding site at an / intersubunit interface. Altogether, our data unveil heteromeric GluClR assemblies having three and two ß subunits arranged in a counterclockwise ß- -ß- - fashion, as viewed from the extracellular side, with either two or three Glu-binding site interfaces. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 5 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Chloride Channels Metabolism Animals Binding Sites CHO Cells Chemistry Genetics Cricetinae Cricetulus Mutation Patch-Clamp Techniques Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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