Exploring the influence of pore shape on conductance and permeation.

ABSTRACT: There are increasing numbers of ion channel structures featuring heteromeric subunit assembly, exemplified by synaptic α1β_B glycine and α4β2 nicotinic receptors. These structures exhibit inherent pore asymmetry, but the relevance of this to function is unknown. Furthermore, molecular dynamics simulations performed on symmetrical homomeric channels often lead to thermal distortion whereby conformations of the resulting ensemble are also asymmetrical. When functionally annotating ion channels, researchers often rely on minimal constrictions determined via radius-profile calculations performed with computer programs, such as HOLE or CHAP, coupled with an assessment of pore hydrophobicity. However, such tools typically employ spherical probe particles, limiting their ability to accu

SUBMITTER: Seiferth D 

PROVIDER: S-EPMC11427812 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature