TY - JOUR T1 - Structural basis for the recognition of the 2019-nCoV by human ACE2 JF - bioRxiv DO - 10.1101/2020.02.19.956946 SP - 2020.02.19.956946 AU - Renhong Yan AU - Yuanyuan Zhang AU - Yingying Guo AU - Lu Xia AU - Qiang Zhou Y1 - 2020/01/01 UR - http://biorxiv.org/content/early/2020/02/20/2020.02.19.956946.abstract N2 - Angiotensin-converting enzyme 2 (ACE2) has been suggested to be the cellular receptor for the new coronavirus (2019-nCoV) that is causing the coronavirus disease 2019 (COVID-19). Like other coronaviruses such as the SARS-CoV, the 2019-nCoV uses the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) to engage ACE2. We most recently determined the structure of the full-length human ACE2 in complex with a neutral amino acid transporter B0AT1. Here we report the cryo-EM structure of the full-length human ACE2 bound to the RBD of the 2019-nCoV at an overall resolution of 2.9 Å in the presence of B0AT1. The local resolution at the ACE2-RBD interface is 3.5 Å, allowing analysis of the detailed interactions between the RBD and the receptor. Similar to that for the SARS-CoV, the RBD of the 2019-nCoV is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. Pairwise comparison reveals a number of variations that may determine the different affinities between ACE2 and the RBDs from these two related viruses. ER -