西湖大学周强课题组揭示了全长人血管紧张素转换酶2（ACE2）识别新冠病毒（SARS-CoV-2）的结构基础。相关论文于2020年3月4日在线发表于《科学》杂志。

Title: Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2

Author: Renhong Yan, Yuanyuan Zhang, Yaning Li, Lu Xia, Yingying Guo, Qiang Zhou

Issue&Volume: 2020/03/04

Abstract: AbstractAngiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a 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 , with a local resolution of 3.5 at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.

DOI: 10.1126/science.abb2762

Source: https://science.sciencemag.org/content/early/2020/03/03/science.abb2762