id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-323828-ug2duzw1	Ni, Dongchun	Structural investigation of ACE2 dependent disassembly of the trimeric SARS-CoV-2 Spike glycoprotein	2020-10-12		.txt	text/plain	3408	234	65	Here we report a single particle cryo-electron microscopy analysis of SARS-CoV-2 trimeric Spike in presence of the human ACE2 ectodomain. The binding of purified hACE2 ectodomain to Spike induces the disassembly of the trimeric form of Spike and a structural rearrangement of its S1 domain to form a stable, monomeric complex with hACE2. The clinical-grade soluble form of hACE2 has been reported to be a 74 potential novel therapeutic approach for reducing the infection of SARS-CoV-2 (Monteil et al., 2020) by preventing the viral Spike from interacting with other hACE2 present on human cells. The final 3D 115 reconstruction from 72'446 particles at 5.1Å overall resolution showed a density map corresponding to a single, 116 monomeric Spike protein in complex with hACE2 (Fig. 1a) . Figure 1 Cryo-EM maps of SARS-CoV-2 Spike-hACE2 complexes and fitted models. Cryo-EM structure of the SARS coronavirus spike glycoprotein in 352 complex with its host cell receptor ACE2	./cache/cord-323828-ug2duzw1.txt	./txt/cord-323828-ug2duzw1.txt