The roles of aromatic residues in the glycine receptor transmembrane domain.

ABSTRACT:

Background

Cys-loop receptors play important roles in fast neuronal signal transmission. Functional receptors are pentamers, with each subunit having an extracellular, transmembrane (TM) and intracellular domain. Each TM domain contains 4 α-helices (M1-M4) joined by loops of varying lengths. Many of the amino acid residues that constitute these α-helices are hydrophobic, and there has been particular interest in aromatic residues, especially those in M4, which have the potential to contribute to the assembly and function of the receptor via a range of interactions with nearby residues.

Results

Here we show that many aromatic residues in the M1, M3 and M4 α-helices of the glycine receptor are involved in the function of the receptor. The residues were explored by creating a r

SUBMITTER: Tang B 

PROVIDER: S-EPMC6127993 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature