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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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
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author Browne, Liam E.
Cao, Lishuang
Broomhead, Helen E.
Bragg, Laricia
Wilkinson, William
North, R. Alan
author_facet Browne, Liam E.
Cao, Lishuang
Broomhead, Helen E.
Bragg, Laricia
Wilkinson, William
North, R. Alan
author_sort Browne, Liam E.
collection PubMed
description 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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spelling pubmed-30120302011-07-01 P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance Browne, Liam E. Cao, Lishuang Broomhead, Helen E. Bragg, Laricia Wilkinson, William North, R. Alan Nat Neurosci Article 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. 2010-12-19 2011-01 /pmc/articles/PMC3012030/ /pubmed/21170052 http://dx.doi.org/10.1038/nn.2705 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Browne, Liam E.
Cao, Lishuang
Broomhead, Helen E.
Bragg, Laricia
Wilkinson, William
North, R. Alan
P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title_full P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title_fullStr P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title_full_unstemmed P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title_short P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
title_sort p2x receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
topic Article
url 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
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