Article
Point mutations of the thyrotropin receptor determining structural requirements for its ability to bind thyrotropin and to stimulate adenylate cyclase activity.
Biochemical and biophysical research communications - 15 Mar 1994
Gustavsson B, Westermark B, Heldin N E
Abstract excerpt
The two cysteines C494 and C569, located in the first and second extracellular loop, respectively, of the thyrotropin (TSH) receptor, were mutated to serines to test the functional significance of the putative disulfide bond between these two cysteines. Single (C494S and C569S) and double (C494/5...
Topics
- Adenylyl Cyclases
- Adult
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Binding, Competitive
- Cell Line
- Cyclic AMP
- Cysteine
- Gene Library
- Genetic Variation
- Graves Disease
- Humans
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Oligodeoxyribonucleotides