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3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1.

Abstract:

ATP-sensitive potassium (K(ATP)) channels conduct potassium ions across cell membranes and thereby couple cellular energy metabolism to membrane electrical activity. Here, we report the heterologous expression and purification of a functionally active K(ATP) channel complex composed of pore-forming Kir6.2 and regulatory SUR1 subunits, and determination of its structure at 18 A resolution by single-particle electron microscopy. The purified channel shows ATP-ase activity similar to that of ATP...

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Publication status:
Published

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Publisher copy:
10.1038/sj.emboj.7600877

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Institution:
University of Oxford
Department:
Oxford, MSD, Physiology Anatomy and Genetics
Role:
Author
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Journal:
The EMBO journal
Volume:
24
Issue:
23
Pages:
4166-4175
Publication date:
2005-12-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:764d4369-31d5-4676-a9d2-a5ce730d83ca
Source identifiers:
92437
Local pid:
pubs:92437

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