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

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...

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Veröffentlicht in:	The EMBO journal 2003-06, Vol.22 (12), p.2903-2912
Hauptverfasser:	Ashcroft, Frances M, Trapp, Stefan, Haider, Shozeb, Jones, Phillippa, Sansom, Mark S.P
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine diphosphate Adenosine Triphosphate - metabolism Amino acids Animals Arginine - chemistry Arginine - metabolism ATP Binding Sites cysteine-scanning electrostatics EMBO20 EMBO27 Ethyl Methanesulfonate - analogs & derivatives Ethyl Methanesulfonate - metabolism G Protein-Coupled Inwardly-Rectifying Potassium Channels Kir6.2 Lysine - chemistry Lysine - metabolism Mesylates - metabolism Mice Models, Molecular Mutagenesis, Site-Directed Oocytes - physiology Patch-Clamp Techniques potassium channel Potassium Channels, Inwardly Rectifying - chemistry Potassium Channels, Inwardly Rectifying - genetics Potassium Channels, Inwardly Rectifying - metabolism Protein Structure, Secondary Rats Reagents Sulfhydryl Compounds - metabolism Sulfhydryl Reagents - metabolism Xenopus laevis
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