P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance

Liam E. Browne; Lishuang Cao; Helen E. Broomhead; Laricia Bragg; William J. Wilkinson; R. Alan North

doi:10.1038/nn.2705

P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance

Liam E. Browne, Lishuang Cao, Helen E. Broomhead, Laricia Bragg, William J. Wilkinson, R. Alan North

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Abstract

In the closed structure of the P2X cation channel, three Î ±-helical transmembrane domains cross the membrane obliquely. In rat P2X2 receptors, these intersect at Thr339. Replacing Thr339 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 Thr339 from each subunit contributes symmetrically to the open channel permeation pathway. © 2011 Nature America, Inc. All rights reserved.

Original language	English
Pages (from-to)	17-18
Number of pages	1
Journal	Nature Neuroscience
Volume	14
Issue number	1
DOIs	https://doi.org/10.1038/nn.2705
Publication status	Published - Jan 2011

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abstract = "In the closed structure of the P2X cation channel, three {\^I} ±-helical transmembrane domains cross the membrane obliquely. In rat P2X2 receptors, these intersect at Thr339. Replacing Thr339 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 Thr339 from each subunit contributes symmetrically to the open channel permeation pathway. {\textcopyright} 2011 Nature America, Inc. All rights reserved.",

author = "Browne, {Liam E.} and Lishuang Cao and Broomhead, {Helen E.} and Laricia Bragg and Wilkinson, {William J.} and North, {R. Alan}",

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AB - In the closed structure of the P2X cation channel, three Î ±-helical transmembrane domains cross the membrane obliquely. In rat P2X2 receptors, these intersect at Thr339. Replacing Thr339 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 Thr339 from each subunit contributes symmetrically to the open channel permeation pathway. © 2011 Nature America, Inc. All rights reserved.

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P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance

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