Ontology highlight
ABSTRACT:
SUBMITTER: Trapp S
PROVIDER: S-EPMC162134 | biostudies-literature | 2003 Jun
REPOSITORIES: biostudies-literature
Trapp Stefan S Haider Shozeb S Jones Phillippa P Sansom Mark S P MS Ashcroft Frances M FM
The EMBO journal 20030601 12
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 increas ...[more]