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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Site-directed mutagenesis of the human adenosine A2A receptor. Critical involvement of Glu13 in agonist recognition.

A glutamic acid residue in the first transmembrane domain of the human adenosine A2A receptor was mutated to glutamine. Radioligand binding studies on COS-7 cell membranes expressing either the wild-type or the mutant receptor revealed that the affinity of the prototypic agonist CGS21680 (2-[4-[(2-carboxyethyl)phenyl]ethylamino]-5'-N-ethylcarboxamidoadenosine ) for the mutant receptor was 15-fold lower than for the wild-type receptor. This was confirmed in functional studies with intact cells. The EC50 values of CGS21680 for the stimulation of cAMP production differed in a similar way. Antagonists of various chemical structure were equally effective on both mutant and wild-type receptors, thus the mutation selectively diminishes agonist affinity. We propose an indirect perturbation of the binding site, perhaps through a proton transfer mechanism as suggested by molecular modelling.[1]

References

  1. Site-directed mutagenesis of the human adenosine A2A receptor. Critical involvement of Glu13 in agonist recognition. IJzerman, A.P., Von Frijtag Drabbe Künzel, J.K., Kim, J., Jiang, Q., Jacobson, K.A. Eur. J. Pharmacol. (1996) [Pubmed]
 
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