Blockade of ethanol-induced potentiation of glycine receptors by a peptide that interferes with Gbetagamma binding.

ABSTRACT: The large intracellular loop (IL) of the glycine receptor (GlyR) interacts with various signaling proteins and plays a fundamental role in trafficking and regulation of several receptor properties, including a direct interaction with Gbetagamma. In the present study, we found that mutation of basic residues in the N-terminal region of the IL reduced the binding of Gbetagamma to 21 +/- 10% of control. Two basic residues in the C-terminal region, on the other hand, contributed to a smaller extent to Gbetagamma binding. Using docking analysis, we found that both basic regions of the IL bind in nearby regions to the Gbetagamma dimer, within an area of high density of amino acids having an electronegative character. Thereafter, we generated a 17-amino acid peptide with the N-terminal sequence o

SUBMITTER: Guzman L 

PROVIDER: S-EPMC2784719 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature