University of Hertfordshire

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Original languageEnglish
Number of pages8
Pages (from-to)347-54
JournalJournal of Physiology
Journal publication date1 Jun 2004
Volume557
IssuePt 2
DOIs
Publication statusPublished - 1 Jun 2004

Abstract

ATP-sensitive potassium (K(ATP)) channels comprise Kir6.2 and SUR subunits. The site at which ATP binds to mediate K(ATP) channel inhibition lies on Kir6.2, but the potency of block is enhanced by coexpression with SUR1. To assess the structure of the ATP-binding site on Kir6.2, we used a range of adenine nucleotides as molecular measuring sticks to map the internal dimensions of the binding site. We compared their efficacy on Kir6.2-SUR1, and on a truncated Kir6.2 (Kir6.2DeltaC) that expresses in the absence of SUR. We show here that SUR1 modifies the ATP-binding pocket of Kir6.2, by increasing the width of the groove that binds the phosphate tail of ATP, without changing the length of the groove, and by enhancing interaction with the adenine ring.

Notes

Copyright The Physiological Society 2004

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