Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.

ABSTRACT: Cyclic nucleotide-binding domain (CNBD) ion channels are vital for cellular signaling and excitability, with activation regulated by cyclic adenosine- or guanosine-monophosphate (cAMP, cGMP) binding. However, the allosteric mechanisms underlying this activation, particularly the energetics that describe conformational changes within individual domains and between domains, remain unclear. The prokaryotic CNBD channel SthK has been a useful model for better understanding these allosteric mechanisms. Previously, we applied time-resolved transition metal ion Förster resonance energy transfer (tmFRET) to investigate the conformational dynamics and energetics in the CNBD of a soluble C-terminal fragment of the SthK protein, SthK_Cterm (Eggan et al., 2024). Here, we used a similar strat

SUBMITTER: Eggan P 

PROVIDER: S-EPMC12342821 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature