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dc.contributor.author
Bouzat, Cecilia Beatriz
dc.date.available
2016-07-04T21:27:20Z
dc.date.issued
2012-03
dc.identifier.citation
Bouzat, Cecilia Beatriz; New insights into the structural bases of activation of Cys-loop receptors; Elsevier; Journal of Physiology; 106; 1-2; 3-2012; 23-33
dc.identifier.issn
0928-4257
dc.identifier.uri
http://hdl.handle.net/11336/6354
dc.description.abstract
Neurotransmitter receptors of the Cys-loop superfamily mediate rapid synaptic transmission throughout the nervous system, and include receptors activated by ACh, GABA, glycine and serotonin. They are involved in physiological processes, including learning and memory, and in neurological disorders, and they are targets for clinically relevant drugs. Cys-loop receptors assemble either from five copies of one type of subunit, giving rise to homomeric receptors, or from several types of subunits, giving rise to heteromeric receptors. Homomeric receptors are invaluable models for probing fundamental relationships between structure and function. Receptors contain a large extracellular domain that carries the binding sites and a transmembrane region that forms the ion pore. How the structural changes elicited by agonist binding are propagated through a distance of 50Å to the ion channel gate is central to understanding receptor function. Depending on the receptor subtype, occupancy of either two, as in the prototype muscle nicotinic receptor, or three binding sites, as in homomeric receptors, is required for full activation. The conformational changes initiated at the binding sites are propagated to the gate through the interface between the extracellular and transmembrane domains. This region forms a network that relays structural changes from the binding site towards the pore, and also contributes to open channel lifetime and rate of desensitization. Thus, this coupling region controls the beginning and duration of a synaptic response. Here we review recent advances in the molecular mechanism by which Cys-loop receptors are activated with particular emphasis on homomeric receptors.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Sinapsis
dc.subject
Receptores de Neurotransmisores
dc.subject
Canales Ionicos
dc.subject
Patch-Clamp
dc.subject.classification
Biofísica
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
New insights into the structural bases of activation of Cys-loop receptors
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-05-10T14:30:03Z
dc.journal.volume
106
dc.journal.number
1-2
dc.journal.pagination
23-33
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Bouzat, Cecilia Beatriz. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina. Universidad Nacional del Sur; Argentina
dc.journal.title
Journal of Physiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jphysparis.2011.09.012
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphysparis.2011.09.012
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/pmid/21995938
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0928425711000386
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