کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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444653 | 693021 | 2008 | 5 صفحه PDF | دانلود رایگان |
Neuronal nicotinic acetylcholine receptors (nAChRs) are important therapeutic targets for various diseases, including Alzheimer's disease, Parkinson's disease, and schizophrenia, as well as for cessation of smoking. Based on the recently determined crystal structure of the extracellular domain (ECD) of the mouse nAChR α1 subunit complexed with α-bungarotoxin at 1.94 Å resolution, we have constructed three-dimensional models of the ECD of the monomer, homodimer, and homopentamer of the human α7 nAChR and investigated in detail the interface between the two α7 subunits. The docking of the agonist in the ligand-binding pocket of the human α7 dimer was also performed and found consistent with results from labeling and mutagenesis experiments. Since the nAChR ligand-binding site is a useful target for mutagenesis studies and the rational design of drugs against diseases, these models provide useful information for future work.
Journal: Journal of Molecular Graphics and Modelling - Volume 26, Issue 8, June 2008, Pages 1333–1337