Allosteric modulation of dopamine D2Receptors by homocysteine

Agnati, Luigi F., Ferré, Sergi, Genedani, Susanna, Leo, Giuseppina, Guidolin, Diego, Filaferro, Monica, Carriba, Paulina, Casadó, Vicent, Lluis, Carme, Franco, Rafael, Woods, Amina S. and Fuxe, Kjell 2006. Allosteric modulation of dopamine D2Receptors by homocysteine. Journal of Proteome Research 5 (11) , pp. 3077-3083. 10.1021/pr0601382

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Abstract

The present study demonstrates that homocysteine exerts an allosteric modulation of dopamine D2 receptors, reducing the affinity of D2 receptors for agonists but not for antagonists. With mass spectrometry techniques it is shown that, by means of an arginine (Arg)−thiol electrostatic interaction, homocysteine forms noncovalent complexes with the two Arg-rich epitopes of the third intracellular loop of the D2 receptor, one of them involved in adenosine A2A−dopamine D2 receptor heteromerization.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	American Chemical Society
ISSN:	1535-3893
Last Modified:	17 Mar 2021 02:42
URI:	https://orca.cardiff.ac.uk/id/eprint/66913

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