Finely ordered intracellular domain harbors an allosteric site to modulate physiopathological function of P2X3 receptors.

ABSTRACT: P2X receptors, a subfamily of ligand-gated ion channels activated by extracellular ATP, are implicated in various physiopathological processes, including inflammation, pain perception, and immune and respiratory regulations. Structural determinations using crystallography and cryo-EM have revealed that the extracellular three-dimensional architectures of different P2X subtypes across various species are remarkably identical, greatly advancing our understanding of P2X activation mechanisms. However, structural studies yield paradoxical architectures of the intracellular domain (ICD) of different subtypes (e.g., P2X3 and P2X7) at the apo state, and the role of the ICD in P2X functional regulation remains unclear. Here, we propose that the P2X3 receptor's ICD has an apo state conformation sim

SUBMITTER: Lin YY 

PROVIDER: S-EPMC11372093 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature