Functional Coupling of the Gαolf Variant XLGαolf with the Human Adenosine A2A Receptor

@article{Ravyn2006FunctionalCO,
  title={Functional Coupling of the G$\alpha$olf Variant XLG$\alpha$olf with the Human Adenosine A2A Receptor},
  author={Vipa Ravyn and James Robert Bostwick},
  journal={Journal of Receptors and Signal Transduction},
  year={2006},
  volume={26},
  pages={241 - 258}
}
A recently identified novel Gαolf variant, XLGαolf, is shown to functionally couple to the human adenosine A2A receptor (A2AR). In Sf9 cells expressing A2AR, β1, and γ2, co-expression of XLGαolf increased NECA-induced [35S]GTPγS binding from approximately 130% to 300% of basal levels. Pharmacological characteristics of A2AR ligands on these cells were evaluated by using [3H]ZM241385- and [35S]GTPγS- binding assays. The rank order of the equilibrium binding constants (Kd or Ki) of adenosine… 

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References

SHOWING 1-10 OF 52 REFERENCES

Human A2A Adenosine Receptors: High-Affinity Agonist Binding to Receptor-G Protein Complexes Containing Gβ4

TLDR
It is concluded that recombinant hA2AAR can form a high-affinity receptor-G protein complex with αsβ4γ2 that is useful for determining receptor selectivity.

Comparison of CGS 15943, ZM 241385 and SCH 58261 as antagonists at human adenosine receptors

TLDR
Data indicate that SCH 58261 is the most selective A2A antagonist currently available, and the different receptor selectivity of these three chemically related compounds provides useful information to progress with structure-activity relationship studies.

Mutagenesis reveals structure-activity parallels between human A2A adenosine receptors and biogenic amine G protein-coupled receptors.

TLDR
Structure-affinity relationships for ligand binding at the human A2A adenosine receptor have been probed using site-directed mutagenesis in the transmembrane helical domains (TMs) to predict the proximity of bound agonist ligands to TM3, TM5, TM6, and TM7.

Characterization of A2A adenosine receptors in human lymphocyte membranes by [3H]‐SCH 58261 binding

TLDR
Thermodynamic data indicate that [3H]‐SCH 58261 binding to human lymphocytes is entropy and enthalpy‐driven, a finding in agreement with the thermodynamic behaviour of antagonists for rat striatal A2A‐adenosine receptors.

Human A(2A) adenosine receptors: high-affinity agonist binding to receptor-G protein complexes containing Gbeta(4).

TLDR
It is concluded that recombinant hA(2A)AR can form a high-affinity receptor-G protein complex with alpha(s)beta(4)gamma(2) that is useful for determining receptor selectivity.

The effects of saponin on the binding and functional properties of the human adenosine A1 receptor

TLDR
It is hypothesized that long‐lasting adenosine‐receptor‐G protein complexes are present in the CHO membrane preparations, and the existence of these complexes may rationalize the observed kinetics and the increase in 3H‐antagonist binding produced by GTP.

A carboxyl-terminally truncated mutant and nonglycosylated A2a adenosine receptors retain ligand binding.

TLDR
The characterization of a purification-amenable truncated mutant of the canine A2a adenosine receptor is described and it is demonstrated that neither the long carboxyl-terminal tail nor the glycosidic moiety appears to be required for ligand binding.

Glutamate residues in the second extracellular loop of the human A2a adenosine receptor are required for ligand recognition.

TLDR
The data suggest that certain amino acids in the second extracellular loop may be directly or indirectly involved in ligand binding to the human A2a receptor.
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