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J Physiol Volume 557, Number 2, 347-354, June 1, 2004 DOI: 10.1113/jphysiol.2003.059105
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RAPID REPORT

Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2

Michael Dabrowski, Andrei Tarasov and Frances M. Ashcroft

University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK

ATP-sensitive potassium (KATP) channels comprise Kir6.2 and SUR subunits. The site at which ATP binds to mediate KATP 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 (Kir6.2{Delta}C) 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.

(Received 2 December 2003; accepted after revision 3 March 2004; first published online 5 March 2004)
Corresponding author F. M. Ashcroft: University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK. Email: frances.ashcroft{at}physiol.ox.ac.uk




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