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-[[Image:1ott.gif|left|200px]]
+{{Seed}}
+[[Image:1ott.png|left|200px]]
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 {{STRUCTURE_1ott|  PDB=1ott  |  SCENE=  }}
-'''Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex'''
+===Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex===
-==Overview==
+<!--
-ClC channels conduct chloride (Cl-) ions across cell membranes and thereby govern the electrical activity of muscle cells and certain neurons, the transport of fluid and electrolytes across epithelia, and the acidification of intracellular vesicles. The structural basis of ClC channel gating was studied. Crystal structures of wild-type and mutant Escherichia coli ClC channels bound to a monoclonal Fab fragment reveal three Cl- binding sites within the 15-angstrom neck of an hourglass-shaped pore. The Cl- binding site nearest the extracellular solution can be occupied either by a Cl- ion or by a glutamate carboxyl group. Mutations of this glutamate residue in Torpedo ray ClC channels alter gating in electrophysiological assays. These findings reveal a form of gating in which the glutamate carboxyl group closes the pore by mimicking a Cl- ion.
+The line below this paragraph, {{ABSTRACT_PUBMED_12649487}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12649487 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12649487}}
 ==About this Structure==
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 [[Category: Fab complex]]
 [[Category: Ion channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:16:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:25:24 2008''