A heuristic derived from analysis of the ion channel structural proteome permits the rapid identification of hydrophobic gates.

ABSTRACT: Ion channel proteins control ionic flux across biological membranes through conformational changes in their transmembrane pores. An exponentially increasing number of channel structures captured in different conformational states are now being determined; however, these newly resolved structures are commonly classified as either open or closed based solely on the physical dimensions of their pore, and it is now known that more accurate annotation of their conductive state requires additional assessment of the effect of pore hydrophobicity. A narrow hydrophobic gate region may disfavor liquid-phase water, leading to local dewetting, which will form an energetic barrier to water and ion permeation without steric occlusion of the pore. Here we quantify the combined influence of radius and hyd

SUBMITTER: Rao S 

PROVIDER: S-EPMC6628796 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature