The poststructural festivities begin.
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.
Maduke
Merritt
M
Stanford University, Department of Molecular and Cellular Physiology, B155 Beckman Center, 279 Campus Drive, Stanford, California 94305, USA.
Mindell
Joseph A
JA
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
D001426:Bacterial Proteins; C086321:CLC-1 channel; D018118:Chloride Channels