A MODEL OF THE CLOSED FORM OF THE NICOTINIC ACETYLCHOLINE RECEPTOR M2 CHANNEL PORE
SCIE
SCOPUS
- Title
- A MODEL OF THE CLOSED FORM OF THE NICOTINIC ACETYLCHOLINE RECEPTOR M2 CHANNEL PORE
- Authors
- Kim, S; Chamberlain, AK; Bowie, JU
- Date Issued
- 2004-08
- Publisher
- BIOPHYSICAL SOCIETY
- Abstract
- The nicotinic acetylcholine receptor is a neurotransmitter-gated ion channel in the postsynaptic membrane. It is composed of five homologous subunits, each of which contributes one transmembrane helix-the M2 helix-to create the channel pore. The M2 helix from the delta subunit is capable of forming a channel by itself. Although a model of the receptor was recently proposed based on a low-resolution, cryo-electron microscopy density map, we found that the model does not explain much of the other available experimental data. Here we propose a new model of the M2 channel derived solely from helix packing and symmetry constraints. This model agrees well with experimental results from solid-state NMR, chemical reactivity, and mutagenesis experiments. The model depicts the channel pore, the channel gate, and the residues responsible for cation specificity.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/9840
- DOI
- 10.1529/BIOPHYSJ.103
- ISSN
- 0006-3495
- Article Type
- Article
- Citation
- BIOPHYSICAL JOURNAL, vol. 87, no. 2, page. 792 - 799, 2004-08
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