有哪些信誉好的足球投注网站identification of a negative allosteric site on human α4β2 and α3β4 neuronal nicotinic acetylcholine receptors识别负面的别构部位对人类α4β2和α3β4神经元烟碱乙酰胆碱受体.pdfVIP
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identification of a negative allosteric site on human α4β2 and α3β4 neuronal nicotinic acetylcholine receptors识别负面的别构部位对人类α4β2和α3β4神经元烟碱乙酰胆碱受体
Identification of a Negative Allosteric Site on Human a4b2 and a3b4 Neuronal Nicotinic Acetylcholine Receptors 1 2 3 3 2 Ryan E. Pavlovicz , Brandon J. Henderson , Andrew B. Bonnell , R. Thomas Boyd , Dennis B. McKay , Chenglong Li1,4* 1 Biophysics Program, Ohio State University, Columbus, Ohio, United States of America, 2 Division of Pharmacology, College of Pharmacy, Ohio State University, Columbus, Ohio, United States of America, 3 Department of Neuroscience, Ohio State University, Columbus, Ohio, United States of America, 4 Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, Ohio State University, Columbus, Ohio, United States of America Abstract Acetylcholine-based neurotransmission is regulated by cationic, ligand-gated ion channels called nicotinic acetylcholine receptors (nAChRs). These receptors have been linked to numerous neurological diseases and disorders such as Alzheimer’s disease, Parkinson’s disease, and nicotine addiction. Recently, a class of compounds has been discovered that antagonize nAChR function in an allosteric fashion. Models of human a4 b2 and a3b4 nicotinic acetylcholine receptor (nAChR) extracellular domains have been developed to computationally explore the binding of these compounds, including the dynamics and free energy changes associated with ligand binding. Through a blind docking study to multiple receptor conformations, the models were used to determine a putative binding mode for the negative allosteric modulators. This mode, in close proximity to the agonist binding site, is presented in addition to a hypothetical m
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