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The Crystal Structure of Angiotensin II Type 2 Receptor with Endogenous Peptide Hormone.
Structure ( IF 4.4 ) Pub Date : 2019-12-30 , DOI: 10.1016/j.str.2019.12.003 Hidetsugu Asada 1 , Asuka Inoue 2 , Francois Marie Ngako Kadji 3 , Kunio Hirata 4 , Yuki Shiimura 5 , Dohyun Im 1 , Tatsuro Shimamura 1 , Norimichi Nomura 1 , Hiroko Iwanari 6 , Takao Hamakubo 6 , Osamu Kusano-Arai 6 , Hiromi Hisano 1 , Tomoko Uemura 1 , Chiyo Suno 1 , Junken Aoki 7 , So Iwata 8
Structure ( IF 4.4 ) Pub Date : 2019-12-30 , DOI: 10.1016/j.str.2019.12.003 Hidetsugu Asada 1 , Asuka Inoue 2 , Francois Marie Ngako Kadji 3 , Kunio Hirata 4 , Yuki Shiimura 5 , Dohyun Im 1 , Tatsuro Shimamura 1 , Norimichi Nomura 1 , Hiroko Iwanari 6 , Takao Hamakubo 6 , Osamu Kusano-Arai 6 , Hiromi Hisano 1 , Tomoko Uemura 1 , Chiyo Suno 1 , Junken Aoki 7 , So Iwata 8
Affiliation
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Angiotensin II (AngII) is a peptide hormone that plays a key role in regulating blood pressure, and its interactions with the G protein-coupled receptors, AngII type-1 receptor (AT1R) and AngII type-2 receptor (AT2R), are central to its mechanism of action. We solved the crystal structure of human AT2R bound to AngII and its specific antibody at 3.2-Å resolution. AngII (full agonist) and [Sar1, Ile8]-AngII (partial agonist) interact with AT2R in a similar fashion, except at the bottom of the AT2R ligand-binding pocket. In particular, the residues including Met1283.36, which constitute the deep end of the cavity, play important roles in angiotensin receptor (ATR) activation upon AngII binding. These differences that occur upon endogenous ligand binding may contribute to a structural change in AT2R, leading to normalization of the non-canonical coordination of helix 8. Our results will inform the design of more effective ligands for ATRs.
中文翻译：
血管紧张素II 2型受体与内源性肽激素的晶体结构。
血管紧张素II（AngII）是一种肽激素，在调节血压中起关键作用，它与G蛋白偶联受体AngII 1型受体（AT1R）和AngII 2型受体（AT2R）的相互作用至关重要发挥作用的机制。我们以3.2-Å的分辨率解决了与AngII及其特异性抗体结合的人AT2R的晶体结构。AngII（完全激动剂）和[Sar1，Ile8] -AngII（部分激动剂）以类似的方式与AT2R相互作用，除了在AT2R配体结合袋的底部。特别地，构成腔深端的包括Met1283.36在内的残基在AngII结合后在血管紧张素受体（ATR）激活中起重要作用。内源性配体结合后发生的这些差异可能会导致AT2R的结构发生变化，
更新日期：2019-12-30
中文翻译：
血管紧张素II 2型受体与内源性肽激素的晶体结构。
血管紧张素II（AngII）是一种肽激素，在调节血压中起关键作用，它与G蛋白偶联受体AngII 1型受体（AT1R）和AngII 2型受体（AT2R）的相互作用至关重要发挥作用的机制。我们以3.2-Å的分辨率解决了与AngII及其特异性抗体结合的人AT2R的晶体结构。AngII（完全激动剂）和[Sar1，Ile8] -AngII（部分激动剂）以类似的方式与AT2R相互作用，除了在AT2R配体结合袋的底部。特别地，构成腔深端的包括Met1283.36在内的残基在AngII结合后在血管紧张素受体（ATR）激活中起重要作用。内源性配体结合后发生的这些差异可能会导致AT2R的结构发生变化，
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