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dc.contributor.author
Xu, Yechun  
dc.contributor.author
Barrantes, Francisco Jose  
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Luo, Xiaomin  
dc.contributor.author
Chen, Kaixian  
dc.contributor.author
Shen, Jianhua  
dc.contributor.author
Jiang, Hualiang  
dc.date.available
2020-03-20T20:18:53Z  
dc.date.issued
2015-03  
dc.identifier.citation
Xu, Yechun; Barrantes, Francisco Jose; Luo, Xiaomin; Chen, Kaixian; Shen, Jianhua; et al.; Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"; American Chemical Society; Journal of the American Chemical Society; 137; 11; 3-2015; 3992-3992  
dc.identifier.issn
0002-7863  
dc.identifier.uri
http://hdl.handle.net/11336/100505  
dc.description.abstract
The nicotinic acetylcholine receptor (AChR) is the paradigm of ligand-gated ion channels, integral membrane proteins that mediate fast intercellular communication in response to neurotransmitters. A 35-ns molecular dynamics simulation has been performed to explore the conformational dynamics of the entireme membrane-spanning region, including the ion channel pore of the AChR. In the simulation, the 20 transmembrane (TM) segments that comprise the whole TM domain of the receptor were inserted into a large dipalmitoylphosphatidylcholine (DPPC) bilayer. The dynamic behavior of individual TM segments and their corresponding AChR subunit helix bundles was examined in order to assess the contribution of each to the conformational transitions of the whole channel. Asymmetrical and asynchronous motions of the M1-M3 TM segments of each subunit were revealed. In addition, the outermost ring of five M4 TM helices was found to convey the effects exerted by the lipid molecules to the central channel domain. Remarkably, a closed-to-open conformational shift was found to occur in one of the channel ring positions in the time scale of the present simulations, the possible physiological significance of which is discussed.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Chemical Society  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
MOLECULAR DYNAMICS  
dc.subject
ACETYLCHOLINE RECEPTOR  
dc.subject
CHANNEL  
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LIPID-PROTEIN INTERACTION  
dc.subject.classification
Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-03-03T15:08:54Z  
dc.journal.volume
137  
dc.journal.number
11  
dc.journal.pagination
3992-3992  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Washington  
dc.description.fil
Fil: Xu, Yechun. Chinese Academy of Sciences; República de China. Rutgers University; Estados Unidos  
dc.description.fil
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina  
dc.description.fil
Fil: Luo, Xiaomin. Chinese Academy of Sciences; República de China  
dc.description.fil
Fil: Chen, Kaixian. Chinese Academy of Sciences; República de China  
dc.description.fil
Fil: Shen, Jianhua. Chinese Academy of Sciences; República de China  
dc.description.fil
Fil: Jiang, Hualiang. Chinese Academy of Sciences; República de China  
dc.journal.title
Journal of the American Chemical Society  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/jacs.5b02329  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jacs.5b02329