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The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.

Original publication

DOI

10.1126/science.1085028

Type

Journal article

Journal

Science

Publication Date

20/06/2003

Volume

300

Pages

1922 - 1926

Keywords

Amino Acid Sequence, Bacterial Proteins, Binding Sites, Burkholderia pseudomallei, Crystallization, Crystallography, X-Ray, Dimerization, Hydrophobic and Hydrophilic Interactions, Ion Channel Gating, Ion Transport, Models, Molecular, Molecular Sequence Data, Potassium, Potassium Channels, Inwardly Rectifying, Protein Conformation, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary