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腺苷受体的结构特征:从晶体结构到功能

Structural features of adenosine receptors: from crystal to function.

作者信息

Piirainen Henni, Ashok Yashwanth, Nanekar Rahul T, Jaakola Veli-Pekka

机构信息

Department of Biochemistry, University of Oulu, Oulu, Finland.

出版信息

Biochim Biophys Acta. 2011 May;1808(5):1233-44. doi: 10.1016/j.bbamem.2010.05.021. Epub 2010 Jun 2.

Abstract

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 A(2A) receptor was recently solved to 2.6Å 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 A(2A) 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 A(2A) 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.

摘要

细胞外腺苷在许多生理过程中发挥的重要作用是由腺苷类G蛋白偶联受体介导的,这类受体也对拮抗剂咖啡因有反应,咖啡因是世界上使用最广泛的药物。人腺苷A(2A)受体的晶体学模型最近与拮抗剂ZM241385形成复合物并解析到2.6埃,ZM241385因其对腺苷受体的强拮抗作用也被称为“超级咖啡因”。晶体学模型揭示了腺苷A(2A)受体结构一些意想不到且不寻常的特征,这些特征引发了对该受体的新研究以及对现有数据的重新审视。与其他已知的GPCR结构相比,腺苷A(2A)受体有一个独特的配体结合口袋,该口袋几乎垂直于膜平面。配体结合位点突出了螺旋核心以及细胞外环和细胞外结构域中的四个二硫键在腺苷类GPCR识别配体过程中的整体作用。

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