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A structural link between inactivation and block of a K+ channel.

Abstract：

:Gating the ion-permeation pathway in K(+) channels requires conformational changes in activation and inactivation gates. Here we have investigated the structural alterations associated with pH-dependent inactivation gating of the KcsA-Kv1.3 K(+) channel using solid-state NMR spectroscopy in direct reference to electrophysiological and pharmacological experiments. Transition of the KcsA-Kv1.3 K(+) channel from a closed state at pH 7.5 to an inactivated state at pH 4.0 revealed distinct structural changes within the pore, correlated with activation-gate opening and inactivation-gate closing. In the inactivated K(+) channel, the selectivity filter adopts a nonconductive structure that was also induced by binding of a pore-blocking tetraphenylporphyrin derivative. The results establish a structural link between inactivation and block of a K(+) channel in a membrane setting.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Ader C,Schneider R,Hornig S,Velisetty P,Wilson EM,Lange A,Giller K,Ohmert I,Martin-Eauclaire MF,Trauner D,Becker S,Pongs O,Baldus M

doi

10.1038/nsmb.1430

subject

Has Abstract

pub_date

2008-06-01 00:00:00

pages

605-12

issue

6

eissn

1545-9993

issn

1545-9985

pii

nsmb.1430

journal_volume

15

pub_type

杂志文章

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