Structure and gating mechanism of the α7 nicotinic acetylcholine receptor.

Amino Acid Sequence Binding Sites Bungarotoxins / chemistry Calcium / metabolism Cell Membrane / chemistry Cryoelectron Microscopy Extracellular Vesicles / metabolism HEK293 Cells Humans Molecular Dynamics Simulation Mutagenesis, Site-Directed Patch-Clamp Techniques Protein Domains Recombinant Proteins / biosynthesis alpha7 Nicotinic Acetylcholine Receptor / chemistry
Cys-loop receptor acetylcholine receptor cryo-EM ion channel ligand-gated ion channel nicotinic receptor α7

Journal

Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066

Informations de publication

Date de publication:
15 04 2021
Historique:
received: 13 11 2020
revised: 13 01 2021
accepted: 22 02 2021
pubmed: 19 3 2021
medline: 21 10 2021
entrez: 18 3 2021
Statut: ppublish

Résumé

The α7 nicotinic acetylcholine receptor plays critical roles in the central nervous system and in the cholinergic inflammatory pathway. This ligand-gated ion channel assembles as a homopentamer, is exceptionally permeable to Ca

Identifiants

DOI: 10.1016/j.cell.2021.02.049 PMID: 33735609 PMC: PMC8135066
pubmed: 33735609
pii: S0092-8674(21)00238-5
doi: 10.1016/j.cell.2021.02.049
pmc: PMC8135066
mid: NIHMS1683166
pii:
doi:

Substances chimiques

Bungarotoxins 0
Recombinant Proteins 0
alpha7 Nicotinic Acetylcholine Receptor 0
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

2121-2134.e13

Subventions

Organisme : NINDS NIH HHS
ID : R01 NS094124
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS095899
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS120496
Pays : United States
Organisme : NINDS NIH HHS
ID : R00 NS077983
Pays : United States
Organisme : NINDS NIH HHS
ID : K99 NS077983
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM129547
Pays : United States

Informations de copyright

Copyright © 2021 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Colleen M Noviello (CM)

Department of Neuroscience, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Anant Gharpure (A)

Department of Neuroscience, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Nuriya Mukhtasimova (N)

Receptor Biology Laboratory, Department of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, Rochester, MN 55902, USA.

Rico Cabuco (R)

Department of Neuroscience, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Leah Baxter (L)

Department of Neuroscience, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Dominika Borek (D)

Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Steven M Sine (SM)

Receptor Biology Laboratory, Department of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, Rochester, MN 55902, USA; Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic College of Medicine, Rochester, MN 55902, USA; Department of Neurology, Mayo Clinic College of Medicine, Rochester, MN 55902, USA.

Ryan E Hibbs (RE)

Department of Neuroscience, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: ryan.hibbs@utsouthwestern.edu.

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Classifications MeSH

questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Structure and gating mechanism of the α7...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Structure and gating mechanism of the α7...
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questionsmedicales.fr › Facteurs biologiques › Facteurs de la coagulation sanguine › Calcium › Structure and gating mechanism of the α7...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › Structure and gating mechanism of the α7...
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › Structure and gating mechanism of the α7...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace extracellulaire › Vésicules extracellulaires › Structure and gating mechanism of the α7...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HEK293 › Structure and gating mechanism of the α7...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Structure and gating mechanism of the α7...
questionsmedicales.fr › Sciences de l'information › Méthodologies informatiques › Simulation numérique › Simulation de dynamique moléculaire › Structure and gating mechanism of the α7...
questionsmedicales.fr › Techniques d'investigation › Techniques génétiques › Génie génétique › Ingénierie des protéines › Mutagenèse dirigée › Structure and gating mechanism of the α7...
questionsmedicales.fr › Techniques d'investigation › Techniques cytologiques › Techniques de patch-clamp › Structure and gating mechanism of the α7...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Structure and gating mechanism of the α7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines recombinantes › Structure and gating mechanism of the α7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs aux neuromédiateurs › Récepteurs cholinergiques › Récepteurs nicotiniques › Récepteur nicotinique de l'acétylcholine alpha7 › Structure and gating mechanism of the α7...