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Abstract：
Functional advances have guided our knowledge of physiological and fatal pathological mechanisms of the hormone angiotensin II (AngII) and its antagonists. Such studies revealed that tissue response to a given dose of the hormone or its antagonist depends on receptors that engage the ligand. Thus, we need to know much more about the structures of receptor-ligand complexes at high resolution. Recently, X-ray structures of both AngII receptors (AT1 and AT2 receptors) bound to peptide and non-peptide ligands have been elucidated, providing new opportunities to examine the dynamic fluxes in the 3D architecture of the receptors, as the basis of ligand selectivity, efficacy, and regulation of the molecular functions of the receptors. Constituent structural motifs cooperatively transform ligand selectivity into specific functions, thus conceptualizing the primacy of the 3D structure over individual motifs of receptors. This review covers the new data elucidating the structural dynamics of AngII receptors and how structural knowledge can be transformative in understanding the mechanisms underlying the physiology of AngII.
摘要：
功能的进步指导了我们对激素血管紧张素II（AngII）及其拮抗剂的生理和致命病理机制的了解。这些研究表明，组织对给定剂量的激素或其拮抗剂的反应取决于与配体结合的受体。因此，我们需要更多地了解高分辨率的受体-配体复合物的结构。最近,已经阐明了与肽和非肽配体结合的两种AngII受体（AT1和AT2受体）的X射线结构，提供新的机会来检查受体3D结构中的动态通量，作为配体选择性的基础，功效,和调节受体的分子功能。组成结构基序协同将配体选择性转化为特定功能，从而概念化3D结构在受体个体基序上的首要地位。这篇综述涵盖了阐明AngII受体结构动力学的新数据，以及结构知识如何在理解AngII生理学基础机制方面具有变革性。
