P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance

In the closed structure of the P2X cation channel, three α-helical transmembrane domains cross the membrane obliquely: in rat P2X2 receptors, these intersect at Thr(339). Replacing Thr(339) by lysine in one, two or three subunits progressively increased chloride permeability and reduced unitary cond...

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Detalles Bibliográficos
Autores principales: Browne, Liam E., Cao, Lishuang, Broomhead, Helen E., Bragg, Laricia, Wilkinson, William, North, R. Alan
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3012030/
https://www.ncbi.nlm.nih.gov/pubmed/21170052
http://dx.doi.org/10.1038/nn.2705
Descripción
Sumario:In the closed structure of the P2X cation channel, three α-helical transmembrane domains cross the membrane obliquely: in rat P2X2 receptors, these intersect at Thr(339). Replacing Thr(339) by lysine in one, two or three subunits progressively increased chloride permeability and reduced unitary conductance. This implies that the closed-open transition involves a symmetrical separation of the three subunits, and that Thr(339) from each contributes symmetrically to the open channel permeation pathway.

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