dc.creatorBasso, Claudia
dc.creatorLabarca, Pedro
dc.creatorStefani, Enrico
dc.creatorAlvarez, Osvaldo
dc.creatorLatorre, Ramón
dc.date.accessioned2018-12-20T14:32:27Z
dc.date.available2018-12-20T14:32:27Z
dc.date.created2018-12-20T14:32:27Z
dc.date.issued1998
dc.identifierFEBS Letters, Volumen 429, Issue 3, 2018, Pages 375-380
dc.identifier00145793
dc.identifier10.1016/S0014-5793(98)00635-8
dc.identifierhttps://repositorio.uchile.cl/handle/2250/156395
dc.description.abstractShaker K+ channels inactivate through two distinct molecular mechanisms: N-type, which involves the N-terminal domain and C-type that appears to involve structural modifications at the external mouth of the channel. We have tested pore accessibility of the Shaker K+ channel during C-type inactivation using Ba2+ as a probe. We determined that external Ba2+ binds to C-type inactivated channels forming an extremely stable complex; i.e. there is Ba2+ trapping by C-type inactivated channels. The structural changes Shaker channels undergo during C-type inactivation create high energy barriers that hinder Ba2+ exit to either the extracellular solution or to the intracellular solution.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceFEBS Letters
dc.subjectBa2+block
dc.subjectPore accessibility
dc.subjectShaker K+channel
dc.subjectSlow inactivation
dc.titlePore accessibility during C-type inactivation in Shaker K+ channels
dc.typeArtículo de revista


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