Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"

Autores
Xu, Yechun; Barrantes, Francisco Jose; Luo, Xiaomin; Chen, Kaixian; Shen, Jianhua; Jiang, Hualiang
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Xu, Yechun. Chinese Academy of Sciences; República de China. Rutgers University; Estados Unidos
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
Fil: Luo, Xiaomin. Chinese Academy of Sciences; República de China
Fil: Chen, Kaixian. Chinese Academy of Sciences; República de China
Fil: Shen, Jianhua. Chinese Academy of Sciences; República de China
Fil: Jiang, Hualiang. Chinese Academy of Sciences; República de China
Materia
MOLECULAR DYNAMICS
ACETYLCHOLINE RECEPTOR
CHANNEL
LIPID-PROTEIN INTERACTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/100505
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"Xu, YechunBarrantes, Francisco JoseLuo, XiaominChen, KaixianShen, JianhuaJiang, HualiangMOLECULAR DYNAMICSACETYLCHOLINE RECEPTORCHANNELLIPID-PROTEIN INTERACTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.Fil: Xu, Yechun. Chinese Academy of Sciences; República de China. Rutgers University; Estados UnidosFil: 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; ArgentinaFil: Luo, Xiaomin. Chinese Academy of Sciences; República de ChinaFil: Chen, Kaixian. Chinese Academy of Sciences; República de ChinaFil: Shen, Jianhua. Chinese Academy of Sciences; República de ChinaFil: Jiang, Hualiang. Chinese Academy of Sciences; República de ChinaAmerican Chemical Society2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/100505Xu, 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; 3992-39920002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/jacs.5b02329info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jacs.5b02329info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:20:40Zoai:ri.conicet.gov.ar:11336/100505instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:20:41.106CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
title Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
spellingShingle Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
Xu, Yechun
MOLECULAR DYNAMICS
ACETYLCHOLINE RECEPTOR
CHANNEL
LIPID-PROTEIN INTERACTION
title_short Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
title_full Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
title_fullStr Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
title_full_unstemmed Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
title_sort Correction to "Conformational Dynamics of the Nicotinic Acetylcholine Receptor Channel: A 35-ns Molecular Dynamics Simulation Study"
dc.creator.none.fl_str_mv Xu, Yechun
Barrantes, Francisco Jose
Luo, Xiaomin
Chen, Kaixian
Shen, Jianhua
Jiang, Hualiang
author Xu, Yechun
author_facet Xu, Yechun
Barrantes, Francisco Jose
Luo, Xiaomin
Chen, Kaixian
Shen, Jianhua
Jiang, Hualiang
author_role author
author2 Barrantes, Francisco Jose
Luo, Xiaomin
Chen, Kaixian
Shen, Jianhua
Jiang, Hualiang
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv MOLECULAR DYNAMICS
ACETYLCHOLINE RECEPTOR
CHANNEL
LIPID-PROTEIN INTERACTION
topic MOLECULAR DYNAMICS
ACETYLCHOLINE RECEPTOR
CHANNEL
LIPID-PROTEIN INTERACTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Xu, Yechun. Chinese Academy of Sciences; República de China. Rutgers University; Estados Unidos
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
Fil: Luo, Xiaomin. Chinese Academy of Sciences; República de China
Fil: Chen, Kaixian. Chinese Academy of Sciences; República de China
Fil: Shen, Jianhua. Chinese Academy of Sciences; República de China
Fil: Jiang, Hualiang. Chinese Academy of Sciences; República de China
description 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/100505
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
0002-7863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100505
identifier_str_mv 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
0002-7863
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/jacs.5b02329
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jacs.5b02329
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781701047451648
score 12.982451

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