Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
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DOI：
10.1126/science.abb2762
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发表时间：
2020-03-27
期刊：
影响因子：
56.9
通讯作者：
Zhou, Qiang
中科院分区：
文献类型：
--
作者：
Yan, Renhong;Zhang, Yuanyuan;Zhou, Qiang
血管紧张素转换酶2（ACE 2）是严重急性呼吸道综合征冠状病毒（SARS-CoV）和导致2019年严重冠状病毒病（COVID-19）流行的新型冠状病毒（SARS-CoV-2）的细胞受体。在这里，我们提出了冷冻电子显微镜结构的全长人类ACE 2的中性氨基酸转运蛋白B 0AT 1的存在下，或没有受体结合结构域（RBD）的表面刺突糖蛋白（S蛋白）的SARS-CoV-2，无论是在2.9埃的整体分辨率，与局部分辨率为3.5埃的ACE 2-RBD接口。ACE 2-B 0AT 1复合物组装为异二聚体的二聚体，ACE 2的聚集蛋白样结构域介导同源二聚化。RBD主要通过极性残基被ACE 2的胞外肽酶结构域识别。这些发现为冠状病毒识别和感染的分子基础提供了重要的见解。
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndromecoronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.