title: The poststructural festivities begin.
abstract: ClC chloride channels orchestrate the movement of chloride necessary for proper neuronal, muscular, cardiovascular, and epithelial function. In this issue of Neuron, Jentsch, Pusch, and colleagues use the structure of a bacterial ClC homolog to guide a mutagenic analysis of inhibitor binding to ClC-0, ClC-1, and ClC-2.
authors.affiliation: Stanford University, Department of Molecular and Cellular Physiology, B155 Beckman Center, 279 Campus Drive, Stanford, California 94305, USA.
authors.forename: Merritt
authors.initials: M
authors.lastname: Maduke
authors.forename: Joseph A
authors.initials: JA
authors.lastname: Mindell
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D001665:Binding Sites; D018118:Chloride Channels / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; C086321:CLC-1 channel; D018118:Chloride Channels