A highly conserved tryptophan residue in the fourth transmembrane domain of the A adenosine receptor is essential for ligand binding but not receptor homodimerization.

Abstract

Dimerization between G protein-coupled receptors (GPCRs) is a clearly established phenomenon. However, limited information is currently available on the interface essential for this process. Based on structural comparisons and sequence homology between rhodopsin and A(1) adenosine receptor (A(1)R), we initially hypothesized that four residues in… (More)
DOI: 10.1111/j.1471-4159.2009.06227.x

Topics

Cite this paper

@article{Suzuki2009AHC, title={A highly conserved tryptophan residue in the fourth transmembrane domain of the A adenosine receptor is essential for ligand binding but not receptor homodimerization.}, author={Tokiko Suzuki and Kazunori Namba and Ryosuke Yamagishi and Hiroki Kaneko and Tatsuya Haga and Hiroyasu Nakata}, journal={Journal of neurochemistry}, year={2009}, volume={110 4}, pages={1352-62} }