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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/100505
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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 Técnicas2025-09-29T09:51:20Zoai: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:34982025-09-29 09:51:20.957CONICET 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 |
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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 |
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1844613578666016768 |
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13.070432 |