Mapping the contribution of the C-linker domain to gating polarity in CNBD channels.

ABSTRACT: Ion channels of the cyclic nucleotide-binding domain (CNBD) family play a crucial role in the regulation of key biological processes, such as photoreception and pacemaking activity in the heart. These channels exhibit high sequence and structural similarity but differ greatly in their functional responses to membrane potential. The CNBD family includes hyperpolarization-activated ion channels and depolarization-activated ether-à-go-go channels. Structural and functional studies show that the differences in the coupling interface between these two subfamilies' voltage-sensing domain and pore domain may underlie their differential response to membrane polarity. However, other structural components may also contribute to defining the polarity differences in activation. Here, we focus on the r

SUBMITTER: Lin JL 

PROVIDER: S-EPMC11309966 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature