Modeling the pore structure of voltage-gated sodium channels in closed, open, and fast-inactivated conformation reveals details of site 1 toxin and local anesthetic binding期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Modeling the pore structure of voltage-gated sodium channels in closed, open, and fast-inactivated conformation reveals details of site 1 toxin and local anesthetic binding

Authors:	Holger Scheib Iain McLay Nicolas Guex Jeff J. Clare Frank E. Blaney Tim J. Dale Simon N. Tate Graeme M. Robertson

Affiliation:	(1) SBC Lab AG, Seebüelstrasse 26, 8185 Winkel, Switzerland;(2) Department of Structural Biology and Bioinformatics, University of Geneva, 1, rue Michel-Servet, 1211 Geneva 4, Switzerland;(3) Swiss Institute of Bioinformatics, Centre Médicale Universitaire, 1, rue Michel-Servet, 1211 Geneva 4, Switzerland;(4) GlaxoSmithKline Medicines Research Centre, Gunnels Wood Road, SG1 2NY Stevenage, Hertfordshire, UK;(5) GlaxoSmithKline, Five Moore Drive, Research Triangle Park, NC 27709, USA;(6) GlaxoSmithKline New Frontiers Science Park (North), Third Avenue, Harlow, Essex, CM19 5AW, UK;(7) sienabiotech SpA, via Fiorentina 1, 53100 Siena, Italy

Abstract:

Keywords:	Voltage-gated sodium channels Tetrodotoxin Tetracaine Protein structure modeling Computational docking
本文献已被 PubMed SpringerLink 等数据库收录！