Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors

Abstract

Purinergic P2X receptors, activated by extracellular ATP, play a role in pain sensation and immune response. We studied the structure of the first transmembrane domains of the P2X4 receptor, and functional role of conserved tyrosine and other aromatic amino acids in five subtypes of P2X family.

We found that aromatic residues contribute to regulation of agonist binding at P2X1, P2X2, P2X3, P2X4 and P2X7 receptors, and play an important role in channel gating.

Keywords

• Purinergic receptors
• gating
• transmembrane domain