Article
Identification of cytoplasmic domains of hVPAC1 receptor required for activation of adenylyl cyclase. Crucial role of two charged amino acids strictly conserved in class II G protein-coupled receptors.
The Journal of biological chemistry - 4 Jul 2003
Couvineau Alain, Lacapere Jean-Jacques, Tan Yossan-Var, Rouyer-Fessard Christiane, Nicole Pascal, Laburthe Marc
Abstract excerpt
The VPAC1 receptor mediates the action of two neuropeptides, vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating peptide. It is a class II G protein-coupled receptor-activating adenylyl cyclase (AC). The role of the N-terminal extracellular domain of hVPAC1 receptor for VIP binding is now established (Laburthe, M., Couvineau, A. and Marie, J. C. (2002) Recept. Channels 8, 137-153), but...
Topics
- Adenylyl Cyclases
- Animals
- CHO Cells
- Cricetinae
- Enzyme Activation
- Humans
- Mutation
- Protein Structure, Tertiary
- Receptors, Vasoactive Intestinal Peptide
- Receptors, Vasoactive Intestinal Polypeptide, Type I
- Signal Transduction
- Structure-Activity Relationship