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. Author manuscript; available in PMC: 2013 Jan 12.
Published in final edited form as: J Med Chem. 2011 Dec 12;55(1):538–552. doi: 10.1021/jm201461q

Figure 2.

Figure 2

Docking poses of 4 (panel A and B, with carbon atoms colored in green and orange) and 14 (panel C, with carbons colored in yellow) in the binding site of the agonist-bound 1-A2AAR structure. The key H-bond interactions between the compounds and the residues of the binding pocket are highlighted as dotted lines. Adenosine 4 may assume an orientation of the 5’-OH group that points toward H250, like the docking mode in panel A, or with the 5’-OH group pointing and interacting with T88, docking mode in panel B. The uronamide group of 14 interacts with both H250 and T88. The H-bond interactions between the adenosine moiety of the agonists and the key residues N253, S277, and H278 as well the hydrophobic interactions with F268, L249, I274 are believed to be conserved for all the agonists in our list.

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