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

P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance.
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DOI:
10.1038/nn.2705
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发表时间:
2011-01
影响因子:
25
通讯作者:
North, R. Alan
North, R. Alan
中科院分区:
医学1区
文献类型:
--
作者:
Browne, Liam E.;Cao, Lishuang;Broomhead, Helen E.;Bragg, Laricia;Wilkinson, William J.;North, R. Alan

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在P2 X阳离子通道的封闭结构中,三个α螺旋跨膜结构域斜向穿过膜:在大鼠P2 X2受体中,它们在Thr 339处相交。替换Thr 339赖氨酸在一个,两个或三个亚基逐步增加氯渗透性和单位电导降低。这意味着封闭-开放过渡涉及三个亚基的对称分离,并且来自每个亚基的Thr 339对称地贡献于开放通道渗透途径。
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 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 contributes symmetrically to the open channel permeation pathway.
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