The Structure of the Adenosine Receptors

Adenosine and adenosine receptors in the immunopathogenesis and treatment of cancer

“…In human, A1R is mainly expressed in the central nervous system (CNS), whereas A2BR and A3R are expressed mainly peripherally and involved in inflammation and immune responses. A2AR is expressed in both the CNS and peripheral, so it can regulate both the neurologic and immunologic responses (Fredholm, Chen, Masino, & Vaugeois, ; Haskó, Csóka, Németh, Vizi, & Pacher, ; Lane, Jaakola, & IJzerman, ; Linden, ; Ohta & Sitkovsky, ). It has been shown that various classes of proteins including serine‐threonine or tyrosine protein kinases, β‐arrestins and scaffolding proteins can bind to ARs (Ciruela et al, ).…”

The role of purinergic pathways in the pathophysiology of gut diseases: Pharmacological modulation and potential therapeutic applications

“…Subsequently, in the late 1980s, several lines of evidence substantiated the existence of a nucleotide receptor, common to ATP and UTP, through the demonstration of a modulating role played by extracellular UTP in the regulation of cell functions, and the identification of a subset of P2Y receptors (P2Y 2 , P2Y 4 and P2Y 6 ) which are able to recognize uridine nucleotides as potent agonists (Häussinger et al, 1987;Lazarowski & Boucher, 2001;von Kügelgen et al, 1987). The biological actions of adenosine, the most relevant catabolite yielded by ATP degradation, are mediated by G-protein-coupled receptors currently distinguished into four subtypes: A 1 , A 2A , A 2B and A 3 (Antonioli et al, 2008a;Fredholm et al, 2001;Jacobson & Gao, 2006;Lane et al, 2011).…”

Molecular Determinants of CGS21680 Binding to the Human Adenosine A2A Receptor

“…Most of the residues of the orthosteric binding site engaged by adenosine are conserved between the different receptor subtypes (Lane et al, 2011;Lebon et al, 2011b). It is consequently difficult to design selective ligands for an adenosine receptor subtype, unless extensions are made into regions of the receptor that are less well conserved, although recently structure-based drug design has facilitated the development of A 2A R-specific ligands that bind deeply in the orthosteric binding pocket .…”