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Journal article

Identification of residues contributing to the ATP binding site of Kir6.2.

Abstract:

The ATP-sensitive potassium (K(ATP)) channel links cell metabolism to membrane excitability. Intracellular ATP inhibits channel activity by binding to the Kir6.2 subunit of the channel, but the ATP binding site is unknown. Using cysteine-scanning mutagenesis and charged thiol-modifying reagents, we identified two amino acids in Kir6.2 that appear to interact directly with ATP: R50 in the N-terminus, and K185 in the C-terminus. The ATP sensitivity of the R50C and K185C mutant channels was incr...

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Publication status:
Published

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Publisher copy:
10.1093/emboj/cdg282

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Institution:
University of Oxford
Division:
MSD
Department:
Physiology Anatomy & Genetics
Role:
Author
Journal:
EMBO journal
Volume:
22
Issue:
12
Pages:
2903-2912
Publication date:
2003-06-01
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
Source identifiers:
100808

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