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Crystal Structure of the Potassium Channel KirBac1.1 in the Closed State
Anling Kuo,1
Jacqueline M. Gulbis,2
Jennifer F. Antcliff,3
Tahmina Rahman,1
Edward D. Lowe,1
Jochen Zimmer,1
Jonathan Cuthbertson,1
Frances M. Ashcroft,3
Takayuki Ezaki,4
Declan A. Doyle1*
Abstract:
The KirBac1.1 channel belongs to the inward-rectifier familyof potassium channels. Here we report the structure of the entireprokaryotic Kir channel assembly, in the closed state, refinedto a resolution of 3.65 angstroms. We identify the main activationgate and structural elements involved in gating. On the basisof structural evidence presented here, we suggest that gatinginvolves coupling between the intracellular and membrane domains.This further suggests that initiation of gating by membraneor intracellular signals represents different entry points toa common mechanistic pathway.
1 University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK. 2 Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia. 3 University of Oxford, University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK. 4 Department of Microbiology and Bioinformatics, Gifu University Graduate School of Medicine, Regeneration, and Advanced Medical Science, 40 Tsukasamachi, Gifu 500-8705, Japan.
* To whom correspondence should be addressed. E-mail: declan{at}biop.ox.ac.uk
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