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Dimers of the neuropeptide Y (NPY) Y2 receptor show asymmetry in agonist affinity and association with G proteins
- Source :
- Journal of receptor and signal transduction research. 28(5)
- Publication Year :
- 2008
-
Abstract
- In conditions precluding activation of G proteins, the binding of agonists to dimers of the neuropeptide Y (NPY) Y2 receptor shows two components of similar size, but differing in affinity. The dimers of all NPY receptors are solubilized as approximately 180-kDa complexes containing one G protein alpha beta gamma trimer. These heteropentamers are stable to excess agonists, chelators, and alkylators. However, dispersion in the weak surfactant cholate releases approximately 300-kDa complexes. These findings indicate that both protomers in the Y2 dimer are associated with G protein heterotrimers, but the extent of interaction depends on affinity for the agonist peptide. The G protein in contact with the first-liganded, higher-affinity protomer should have a stronger interaction with the receptor and a larger probability of activation.
- Subjects :
- Agonist
G protein
medicine.drug_class
Stereochemistry
Phosphodiesterase Inhibitors
Dimer
Trimer
Protomer
CHO Cells
Biochemistry
chemistry.chemical_compound
Mice
Cricetulus
GTP-Binding Proteins
Cricetinae
medicine
Animals
Humans
Estrenes
Receptor
Molecular Biology
G protein-coupled receptor
Cell Biology
Neuropeptide Y receptor
Pyrrolidinones
Receptors, Neuropeptide Y
chemistry
Guanosine 5'-O-(3-Thiotriphosphate)
Rabbits
Protein Multimerization
Subjects
Details
- ISSN :
- 15324281
- Volume :
- 28
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Journal of receptor and signal transduction research
- Accession number :
- edsair.doi.dedup.....ad9fa82045004a650da425390903b7cc