CLC chloride channels: correlating structure with function |
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Authors: | Estévez Raúl Jentsch Thomas J |
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Institution: | 1. Centre de Recherches sur la Cognition Animale, Université Paul Sabatier Toulouse III, 118 route de Narbonne, F-31062 Toulouse Cedex 9, France;2. Laboratoire Récepteurs et Canaux Ioniques Membranaires (RCIM), UPRES-EA2647 USC INRA 1330 SFR 4207 QUASAV, LUNAM Université d''Angers, 2 blvd Lavoisier, F-49045 Angers Cedex 01, France |
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Abstract: | CLC chloride channels form a large gene family that is found in bacteria, archae and eukaryotes. Previous mutagenesis studies on CLC chloride channels, combined with electrophysiology, strongly supported the theory that these channels form a homodimeric structure with one pore per subunit (a'double-barrelled' channel), and also provided clues about gating and permeation. Recently, the crystal structures of two bacterial CLC proteins have been obtained by X-ray diffraction analysis. They confirm the double-barrelled architecture, and reveal a surprisingly complex and unprecedented channel structure. At its binding site in the pore, chloride interacts with the ends of four helices that come from both sides of the membrane. A glutamate residue that protrudes into the pore is proposed to participate in gating. The structure confirms several previous conclusions from mutagenesis studies and provides an excellent framework for their interpretation. |
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