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

被引：36

作者：

Browne, Liam E. ^{[1
,2
]}

Cao, Lishuang ^{[1
,2
]}

Broomhead, Helen E. ^{[1
,2
]}

Bragg, Laricia ^{[1
,2
]}

Wilkinson, William J. ^{[1
,2
]}

North, R. Alan ^{[1
,2
]}

机构：

[1] Univ Manchester, Fac Med & Human Sci, Manchester, Lancs, England

[2] Univ Manchester, Fac Life Sci, Manchester, Lancs, England

来源：

NATURE NEUROSCIENCE | 2011年 / 14卷 / 01期

基金：

英国惠康基金;

关键词：

2ND TRANSMEMBRANE DOMAIN; POLAR RESIDUES; PORE; RECTIFICATION;

D O I：

10.1038/nn.2705

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

In the closed structure of the P2X cation channel, three alpha-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 subunit contributes symmetrically to the open channel permeation pathway.

引用

页码：17 / 18

页数：2

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