کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1944567 | 1053226 | 2011 | 12 صفحه PDF | دانلود رایگان |

The important role that extracellular adenosine plays in many physiological processes is mediated by the adenosine class of G protein-coupled receptors, a class of receptors that also responds to the antagonist caffeine, the most widely used pharmacological agent in the world. The crystallographic model of the human adenosine A2A receptor was recently solved to 2.6 Å in complex with the antagonist ZM241385, which is also referred to as “super-caffeine” because of its strong antagonistic effect on adenosine receptors. The crystallographic model revealed some unexpected and unusual features of the adenosine A2A receptor structure that have led to new studies on the receptor and the re-examination of pre-existing data. Compared to other known GPCR structures, the adenosine A2A receptor has a unique ligand binding pocket that is nearly perpendicular to the membrane plane. The ligand binding site highlights the integral role of the helical core together with the extracellular loops and the four disulfide bridges in the extracellular domain, in ligand recognition by the adenosine class of GPCRs. This article is part of a Special Issue entitled: “Adenosine Receptors”.
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1808, Issue 5, May 2011, Pages 1233–1244