Science. 2003 Jun 20;300(5627):1922-6. Epub 2003 May 8.

Crystal structure of the potassium channel KirBac1.1 in the closed state.

Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, Doyle DA.

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University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.

Abstract

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.

PMID:: 12738871; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Potassium Channel From Burkholderia Pseudomallei

PDB: 2WLL

Source: Burkholderia pseudomallei

Method: X-Ray Diffraction

Resolution: 3.65 Å

See all 2 structures...

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Crystal structure of the potassium channel KirBac1.1 in the closed state.

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