Intersubunit physical couplings fostered by the left flipper domain facilitate channel opening of P2X4 receptors.

ABSTRACT: P2X receptors are ATP-gated trimeric channels with important roles in diverse pathophysiological functions. A detailed understanding of the mechanism underlying the gating process of these receptors is thus fundamentally important and may open new therapeutic avenues. The left flipper (LF) domain of the P2X receptors is a flexible loop structure, and its coordinated motions together with the dorsal fin (DF) domain are crucial for the channel gating of the P2X receptors. However, the mechanism underlying the crucial role of the LF domain in the channel gating remains obscure. Here, we propose that the ATP-induced allosteric changes of the LF domain enable it to foster intersubunit physical couplings among the DF and two lower body domains, which are pivotal for the channel gating of P2X4 re

SUBMITTER: Wang J 

PROVIDER: S-EPMC5418059 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature