Article
The role of arrestin alpha-helix I in receptor binding.
Journal of molecular biology - 8 Jan 2010
Vishnivetskiy Sergey A, Francis Derek, Van Eps Ned, Kim Miyeon, Hanson Susan M, Klug Candice S, Hubbell Wayne L, Gurevich Vsevolod V
Abstract excerpt
Arrestins rapidly bind phosphorylated activated forms of their cognate G protein-coupled receptors, thereby preventing G protein coupling and often switching signaling to other pathways. Amphipathic alpha-helix I (residues 100-111) has been implicated in receptor binding, but the mechanism of its action has not been determined yet. Here we show that several mutations in the helix itself and in adjacent...
Topics
- Amino Acid Substitution
- Animals
- Arrestin
- Cattle
- Hydrophobic and Hydrophilic Interactions
- Mutation
- Phosphorylation
- Protein Binding
- Protein Structure, Secondary
- Rhodopsin