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| {{STRUCTURE_1kpl| PDB=1kpl | SCENE= }} | | {{STRUCTURE_1kpl| PDB=1kpl | SCENE= }} |
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| '''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
| | ===Crystal Structure of the ClC Chloride Channel from S. typhimurium=== |
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| ==Overview==
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| 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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11796999 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11796999}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Homodimer]] | | [[Category: Homodimer]] |
| [[Category: Ion channel]] | | [[Category: Ion channel]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:01:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:43:16 2008'' |
