Impact of intracellular domain flexibility upon properties of activated human 5-HT3 receptors.

ABSTRACT:

Background and purpose

It has been proposed that arginine residues lining the intracellular portals of the homomeric 5-HT3 A receptor cause electrostatic repulsion of cation flow, accounting for a single-channel conductance substantially lower than that of the 5-HT3 AB heteromer. However, comparison of receptor homology models for wild-type pentamers suggests that salt bridges in the intracellular domain of the homomer may impart structural rigidity, and we hypothesized that this rigidity could account for the low conductance.

Experimental approach

Mutations were introduced into the portal region of the human 5-HT3 A homopentamer, such that putative salt bridges were broken by neutralizing anionic partners. Single-channel and whole cell currents were measured in transfected

SUBMITTER: Kozuska JL 

PROVIDER: S-EPMC3966743 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature