Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin

Abstract

Cysteine-scanning mutagenesis of rat P2X4-TMs was used to identify and map residues of potential importance for channel gating and interaction with IVM.

Keywords

• purinergic signaling
• ATP-gated receptor-channels
• transmembrane domains
• deactivation
• helical wheel projection
• chloride channel
• caenorhabditis-elegans
• cation permeability
• atp
• domain
• avermectin-b1a
• rearrangements
• deactivation
• segments
• trimers