tailieunhanh - Báo cáo y học: " Binding of long-chain α-neurotoxin would stabilize the resting state of nAChR: A comparative study with α-conotoxin"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: "Binding of long-chain α-neurotoxin would stabilize the resting state of nAChR: A comparative study with α-conotoxin | Theoretical Biology and Medical Modelling BioMed Central Research Binding of long-chain a-neurotoxin would stabilize the resting state of nAChR A comparative study with a-conotoxin Adak Nasiripourdori Bijan Ranjbar and Hossein Naderi-Manesh Open Access Address Department of Biophysics Faculty of Science Tarbiat Modares University . Box 14115-175 Tehran Iran Email Adak Nasiripourdori - nasiripour@ Bijan Ranjbar - ranjbarb@ Hossein Naderi-Manesh - naderman@ Corresponding author Published II February 2009 Received 5 June 2008 Theoretical Biology and Medical Modelling 2009 6 3 doi 1742-4682-6-3 Accepted 11 February 2009 This article is available from http content 6 1 3 2009 Nasiripourdori et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The details of interaction in a complex between potent antagonists such as long chain a-neurotoxins and a-conotoxins with nicotinic acetylcholine receptor nAChR and conformational changes induced by these antagonists are not yet clear. Modeling In order to uncover some of these critical structural features we conducted a docking simulation and a molecular dynamics simulation MD of a model of the ligand binding domain of nAChR in complex with a long-chain a-neurotoxin and an a-conotoxin. Results Our docking results confirm the claim that is in the basal or resting state which favors binding to the alpha-neurotoxins. Moreover more correct hits for the a Y interface upon docking for conotoxin-nAChR confirm the preference of conotoxin GI for the a ỵ interface. More importantly upon binding of a-neurotoxin ligand-bonded .