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Authordc.contributor.authorAlcaino, Constanza 
Authordc.contributor.authorMusgaard, Maria 
Authordc.contributor.authorMinguez, Teresa 
Authordc.contributor.authorMazzaferro, Simone 
Authordc.contributor.authorFaundez, Manuel 
Authordc.contributor.authorIturriaga-Vásquez, Patricio 
Authordc.contributor.authorBiggin, Philip C. 
Authordc.contributor.authorBermudez, Isabel 
Admission datedc.date.accessioned2019-03-18T11:55:33Z
Available datedc.date.available2019-03-18T11:55:33Z
Publication datedc.date.issued2017
Cita de ítemdc.identifier.citationJournal of Biological Chemistry, Volumen 292, Issue 2, 2018, Pages 551-562
Identifierdc.identifier.issn1083351X
Identifierdc.identifier.issn00219258
Identifierdc.identifier.other10.1074/jbc.M116.751206
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/166988
Abstractdc.description.abstract© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.Allosteric modulators of pentameric ligand-gated ion channels are thought to act on elements of the pathways that couple agonist binding to channel gating. Using α4β2 nicotinic acetylcholine receptors and the α4β2-selective positive modulators 17-estradiol (βEST) and desformylflustrabromine (dFBr), we have identified pathways that link the binding sites for these modulators to the Cys loop, a region that is critical for channel gating in all pentameric ligand-gated ion channels. Previous studies have shown that the binding site for potentiatingβEST is in the C-terminal (post-M4) region of the α4 subunit. Here, using homology modeling in combination with mutagenesis and electrophysiology, we identified the binding site for potentiating dFBr on the top half of a cavity between the third (M3) and fourth transmembrane (M4) α-helices of the α4 subunit. We found that the binding sites for βEST and dFBr communicate wit
Lenguagedc.language.isoen
Publisherdc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceJournal of Biological Chemistry
Keywordsdc.subjectBiochemistry
Keywordsdc.subjectMolecular Biology
Keywordsdc.subjectCell Biology
Títulodc.titleRole of the cys loop and transmembrane domain in the allosteric modulation of α4β2 nicotinic acetylcholine receptors
Document typedc.typeArtículo de revista
dcterms.accessRightsdcterms.accessRightsAcceso Abierto
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
Indexationuchile.indexArtículo de publicación ISI
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile