The open pore conformation of potassium channels.

Abstract:

:Living cells regulate the activity of their ion channels through a process known as gating. To open the pore, protein conformational changes must occur within a channel's membrane-spanning ion pathway. KcsA and MthK, closed and opened K(+) channels, respectively, reveal how such gating transitions occur. Pore-lining 'inner' helices contain a 'gating hinge' that bends by approximately 30 degrees. In a straight conformation four inner helices form a bundle, closing the pore near its intracellular surface. In a bent configuration the inner helices splay open creating a wide (12 A) entryway. Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K(+) channels, both ligand- and voltage-gated. The open conformation favours high conduction by compressing the membrane field to the selectivity filter, and also permits large organic cations and inactivation peptides to enter the pore from the intracellular solution.

journal_name

Nature

journal_title

Nature

authors

Jiang Y,Lee A,Chen J,Cadene M,Chait BT,MacKinnon R

doi

10.1038/417523a

keywords:

subject

Has Abstract

pub_date

2002-05-30 00:00:00

pages

523-6

issue

6888

eissn

0028-0836

issn

1476-4687

pii

417523a

journal_volume

417

pub_type

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