Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | Spitzmaul, Guillermo Federico | - |
| dc.creator | Corradi, Jeremias | - |
| dc.creator | Bouzat, Cecilia Beatriz | - |
| dc.date | 2018-07-25T17:12:29Z | - |
| dc.date | 2018-07-25T17:12:29Z | - |
| dc.date | 2004-01 | - |
| dc.date | 2018-07-11T14:11:44Z | - |
| dc.date.accessioned | 2019-04-29T15:39:17Z | - |
| dc.date.available | 2019-04-29T15:39:17Z | - |
| dc.date.issued | 2004-01 | - |
| dc.identifier | Spitzmaul, Guillermo Federico; Corradi, Jeremias; Bouzat, Cecilia Beatriz; Mechanistic contributions of residues in the M1 transmembrane domain of the nicotinic receptor to channel gating; Taylor & Francis Ltd; Molecular Membrane Biology; 21; 1; 1-2004; 39-50 | - |
| dc.identifier | 0968-7688 | - |
| dc.identifier | http://hdl.handle.net/11336/53089 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298660 | - |
| dc.description | The nicotinic receptor (AChR) is a pentamer of homologous subunits with an α2βεδ composition in adult muscle. Each subunit contains four transmembrane domains (M1-M4). Position 15′ of the M1 domain is phenylalanine in α subunits while it is isoleucine in non-α subunits. Given this peculiar conservation pattern, we studied its contribution to muscle AChR activation by combining mutagenesis with single-channel kinetic analysis. AChRs containing the mutant α subunit (αF15′I) as well as those containing the reverse mutations in the non-α subunits (βI15′F, δI15′F, and εI15′F) show prolonged lifetimes of the diliganded open channel resulting from a slower closing rate with respect to wild-type AChRs. The kinetic changes are not equivalent among subunits, the β subunit, being the one that produces the most significant stabilization of the open state. Kinetic analysis of βI15′F AChR channels activated by the low-efficacious agonist choline revealed a 10-fold decrease in the closing rate, a 2.5-fold increase in the opening rate, a 28-fold increase in the gating equilibrium constant of the diliganded receptor, and a significant increased opening in the absence of agonist. Mutations at βI15′ showed that the structural bases of its contribution to gating is complex. Rate-equilibrium linear free-energy relationships suggest an ∼70% closed-state-like environment for the β15′ position at the transition state of gating. The overall results identify position 15′ as a subunit-selective determinant of channel gating and add new experimental evidence that gives support to the involvement of the M1 domain in the operation of the channel gating apparatus. | - |
| dc.description | Fil: Spitzmaul, Guillermo Federico. 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: Corradi, Jeremias. 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: Bouzat, Cecilia Beatriz. 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.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Taylor & Francis Ltd | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/09687680310001607341 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1080/09687680310001607341 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/53089 | - |
| dc.subject | ACETYLCHOLINE | - |
| dc.subject | ACETYLCHOLINE RECEPTOR | - |
| dc.subject | ION CHANNEL | - |
| dc.subject | PATCH CLAMP | - |
| dc.subject | SITE-DIRECTED MUTAGENESIS | - |
| dc.subject | Salud Ocupacional | - |
| dc.subject | Ciencias de la Salud | - |
| dc.subject | CIENCIAS MÉDICAS Y DE LA SALUD | - |
| dc.title | Mechanistic contributions of residues in the M1 transmembrane domain of the nicotinic receptor to channel gating | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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