Conformational dynamics of the prokaryotic CNG channel SthK

Abstract

The cyclic nucleotide-binding domain (CNBD) family of ion channels are critical for numerous physiological processes including phototransduction in the retina (CNG channels) and pacemaking in the heart and brain (HCN channels). While protein structures of CNBD channel family members have provided considerable insights into channel architecture, the allosteric mechanism of how cyclic nucleotide binding modulates pore opening is still unknown. Understanding the functional states, number of states, relative energies of the states, and the allowed transitions between them as these channels open is important to better understand the biophysical mechanisms controlling these channels.