Article
Pharmacological characterization of human m1 muscarinic acetylcholine receptors with double mutations at the junction of TM VI and the third extracellular domain.
The Journal of pharmacology and experimental therapeutics - 1 Sept 1998
Huang X P, Williams F E, Peseckis S M, Messer W S
Abstract excerpt
A mutant human m5 receptor containing the mutations of Ser465 to Tyr and Thr466 to Pro showed constitutive activity. By replacing the equivalent Ser388 with Tyr and Thr389 with Pro, we created a mutant human m1 (Hm1) receptor with comparable double mutations. The mutant receptor, Hm1(Ser388Tyr, T...
Topics
- Amino Acid Sequence
- Cell Line
- Humans
- Molecular Sequence Data
- Muscarinic Agonists
- Mutation
- Phosphatidylinositols
- Protein Conformation
- Quinuclidinyl Benzilate
- Receptor, Muscarinic M1
- Receptors, Muscarinic
- Structure-Activity Relationship