Molecular determinants of cesium- and glycine-dependent glycine receptor activation.

ABSTRACT: The neurotransmitter receptor for glycine (GlyR) is a ligand-gated chloride-permeable ion channel in the central nervous system, and dysregulation of this channel is associated with diverse neurological disorders. Cesium (Cs⁺) is an agonist of GlyRs, and recent atomistic molecular dynamic simulations suggested amino acids D141, E192, and D194 with negatively charged side chains as possible binding sites for Cs⁺. To test this hypothesis, we mutated these positions to code for alanine with a neutral hydrophobic side chain or lysine with a positively charged side chain. The correspondingly mutated GlyR channels were expressed in HEK293T cells and analyzed using whole-cell patch clamp electrophysiology. The results show that D141 mutations had no considerable effect on Gl

SUBMITTER: Harnau M 

PROVIDER: S-EPMC12457638 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature