Molecular docking study on the α3β2 neuronal nicotinic acetylcholine receptor complexed with α-Conotoxin GIC

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Title
Molecular docking study on the α3β2 neuronal nicotinic acetylcholine receptor complexed with α-Conotoxin GIC
Author(s)
Chewook Lee; Si Hyoung Lee; D H Kim; Kyou Hoon Han
Bibliographic Citation
BMB Reports, vol. 45, no. 5, pp. 275-280
Publication Year
2012
Abstract
Nicotinic acetylcholine receptors (nAChRs) are a diverse family of homo- or heteropentameric ligand-gated ion channels. Understanding the physiological role of each nAChR subtype and the key residues responsible for normal and pathological states is important. α-Conotoxin neuropeptides are highly selective probes capable of discriminating different subtypes of nAChRs. In this study, we performed homology modeling to generate the neuronal α3, β2 and β4 subunits using the x-ray structure of the α1 subunit as a template. The structures of the extracellular domains containing ligand binding sites in the α3β2 and α3β4 nAChR subtypes were constructed using MD simulations and ligand docking processes in their free and ligand-bound states using α-conotoxin GIC, which exhibited the highest α3β2 vs. α3β4 discrimination ratio. The results provide a reasonable structural basis for such a discriminatory ability, supporting the idea that the present strategy can be used for future investigations on nAChR-ligand complexes.
Keyword
α-Conotoxin GICHomology modelingLigand-dockingMolecular Dynamics (MD) simulationsNicotinic acetylcholine receptors (nAChRs)
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/BMBRep.2012.45.5.275
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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