Article
Mutation of peptide binding site in transmembrane region of a G protein-coupled receptor accounts for endothelin receptor subtype selectivity.
The Journal of biological chemistry - 29 Apr 1994
Krystek S R, Patel P S, Rose P M, Fisher S M, Kienzle B K, Lach D A, Liu E C, Lynch J S, Novotny J, Webb M L
Abstract excerpt
The molecular basis for endothelin (ET) isopeptide selectivity between ETA and ETB receptors was studied by examining ligand binding to several site-specific mutants of the human ETA receptor. Based on a computer-built three-dimensional model of the ETA receptor, five non-conserved amino acids, clustered around the putative ligand binding site, were targeted for mutation to alanine. Expression of the wild-type...
Topics
- Amino Acid Sequence
- Binding Sites
- Cell Line
- Cell Membrane
- GTP-Binding Proteins
- Humans
- Molecular Sequence Data
- Mutation
- Oligopeptides
- Receptors, Endothelin