2r9r | pdb_00002r9r

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Revision as of 09:50, 23 January 2008 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2r9r" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r9r, resolution 2.40Å" /> '''Shaker family voltag...)
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Shaker family voltage dependent potassium channel (kv1.2-kv2.1 paddle chimera channel) in association with beta subunit

File:2r9r.jpg


2r9r, resolution 2.40Å

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Overview

Voltage-dependent K+ (Kv) channels repolarize the action potential in, neurons and muscle. This type of channel is gated directly by membrane, voltage through protein domains known as voltage sensors, which are, molecular voltmeters that read the membrane voltage and regulate the pore., Here we describe the structure of a chimaeric voltage-dependent K+, channel, which we call the 'paddle-chimaera channel', in which the, voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2., Crystallized in complex with lipids, the complete structure at 2.4, angstrom resolution reveals the pore and voltage sensors embedded in a, membrane-like arrangement of lipid molecules. The detailed structure, which can be compared directly to a large body of functional data, explains charge stabilization within the membrane and suggests a mechanism, for voltage-sensor movements and pore gating.

About this Structure

2R9R is a Protein complex structure of sequences from Rattus norvegicus with K, NAP and PGW as ligands. Full crystallographic information is available from OCA.

Reference

Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment., Long SB, Tao X, Campbell EB, MacKinnon R, Nature. 2007 Nov 15;450(7168):376-82. PMID:18004376

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