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Cover picture: Only a handful of residues are highly conserved throughout the CLC family. One of these, a lysine residue on helix E (purple), participates in a hydrogen-bond network with residues that directly coordinate the chloride ions in the pore. Mutation of this lysine in ClC-0 causes a shift in the fast-gate voltage dependence but preserves the sensitivity to extracellular chloride (compare bottom two panels). Analysis of gating kinetics in combination with the available structural information suggest some of the structural changes likely to underpin fast-gate opening (see articles by Engh et al., 335–349 and 351–363).
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