Article
Replacement of lysine-181 by aspartic acid in the third transmembrane region of endothelin type B receptor reduces its affinity to endothelin peptides and sarafotoxin 6c without affecting G protein coupling.
Journal of cellular biochemistry - 1 Oct 1992
Zhu G, Wu L H, Mauzy C, Egloff A M, Mirzadegan T, Chung F Z
Abstract excerpt
A conserved aspartic acid residue in the third transmembrane region of many of the G protein-coupled receptors has been shown to play a role in ligand binding. In the case of endothelin receptors, however, a lysine residue replaces this conserved aspartic acid residue. To access the importance of this residue in ligand binding, we have replaced it with an aspartic acid in the rat endothelin type B (ETb) receptor...
Topics
- Animals
- Aspartic Acid
- Binding, Competitive
- Brain
- DNA
- Endothelins
- GTP-Binding Proteins
- Inositol Phosphates
- Iodine Radioisotopes
- Lysine
- Male