1kpl: Difference between revisions

Revision as of 10:43, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kpl.png

Template:STRUCTURE 1kpl

Crystal Structure of the ClC Chloride Channel from S. typhimuriumCrystal Structure of the ClC Chloride Channel from S. typhimurium

Template:ABSTRACT PUBMED 11796999

About this StructureAbout this Structure

1KPL is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity., Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R, Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999

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OCA

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-'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
+===Crystal Structure of the ClC Chloride Channel from S. typhimurium===
-==Overview==
+<!--
-The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11796999}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11796999}}
 ==About this Structure==
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 [[Category: Homodimer]]
 [[Category: Ion channel]]
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