Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domain

Abstract

Background: ATP-gated (P2X) receptors form pores with second transmembrane helices from each of three subunits. Results: Addition of an unbranched lipophilic group at I328C in P2X2 receptors opened the channel as effectively as ATP. Conclusion: Destabilizing the Ile328/Val48 interaction allows the Ile328 side chain to move laterally and open the pore. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.