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New Structural insights into Kir channel gating from molecular simulations, HDX-MS and functional studies.
Fagnen, Charline; Bannwarth, Ludovic; Oubella, Iman; Forest, Eric; De Zorzi, Rita; de Araujo, Aline; Mhoumadi, Yasmina; Bendahhou, Saïd; Perahia, David; Vénien-Bryan, Catherine.
Afiliación
  • Fagnen C; Sorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005, Paris, France.
  • Bannwarth L; Laboratoire de Biologie et de Pharmacologie Appliquée, Ecole Normale Supérieure Paris-Saclay, Centre National de la Recherche Scientifique, 91190, Gif-sur-Yvette, France.
  • Oubella I; Sorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005, Paris, France.
  • Forest E; Sorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005, Paris, France.
  • De Zorzi R; University Grenoble Alpes, IBS, F-38044 Grenoble, France, CNRS, IBS, F-38044 Grenoble, France, CEA,IBS, F-38044, Grenoble, France.
  • de Araujo A; Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via Licio Giorgeri 1, 34127, Trieste, Italy.
  • Mhoumadi Y; Sorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005, Paris, France.
  • Bendahhou S; Laboratoire de Biologie et de Pharmacologie Appliquée, Ecole Normale Supérieure Paris-Saclay, Centre National de la Recherche Scientifique, 91190, Gif-sur-Yvette, France.
  • Perahia D; Sorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005, Paris, France.
  • Vénien-Bryan C; Laboratoire de Biologie et de Pharmacologie Appliquée, Ecole Normale Supérieure Paris-Saclay, Centre National de la Recherche Scientifique, 91190, Gif-sur-Yvette, France.
Sci Rep ; 10(1): 8392, 2020 05 21.
Article en En | MEDLINE | ID: mdl-32439887
Inward rectifier potassium (Kir) channels play diverse and important roles in shaping action potentials in biological membranes. An increasing number of diseases are now known to be directly associated with abnormal Kir function. However, the gating of Kir still remains unknown. To increase our understanding of its gating mechanism, a dynamical view of the entire channel is essential. Here the gating activation was studied using a recent developped in silico method, MDeNM, which combines normal mode analysis and molecular dynamics simulations that showed for the very first time the importance of interrelated collective and localized conformational movements. In particular, we highlighted the role played by concerted movements of the different regions throughout the entire protein, such as the cytoplasmic and transmembrane domains and the slide helices. In addition, the HDX-MS analysis achieved in these studies provided a comprehensive and detailed view of the dynamics associated with open/closed transition of the Kir channel in coherence with the theoretical results. MDeNM gives access to the probability of the different opening states that are in agreement with our electrophysiological experiments. The investigations presented in this article are important to remedy dysfunctional channels and are of interest for designing new pharmacological compounds.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Rectificación Interna Idioma: En Revista: Sci Rep Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Rectificación Interna Idioma: En Revista: Sci Rep Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido