id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-328189-jpkxjn6e	Brielle, Esther S.	The SARS-CoV-2 exerts a distinctive strategy for interacting with the ACE2 human receptor	2020-03-12		.txt	text/plain	2971	172	53	We compare the interaction between the human ACE2 receptor and the SARS-CoV-2 spike protein with that of other pathogenic coronaviruses using molecular dynamics simulations. Herein, we analyze the binding of several CoV RBDs to ACE2 with molecular dynamics (MD) simulations and compare the stability, relative interaction strength, and dynamics of the interaction between the viral spike protein and the human ACE2 receptor. While the sequence identity between the RBDs of COVID-19 and SARS-2002 is 73% (Table 1) , we observe a significantly higher residue substitution rate at the interaction interface with the ACE2 receptor. Our MD simulation analysis reveals that the SARS-des has a substantially lower interaction scores with ACE2 (median of -2199.2, Fig. S2) , as expected for an optimized human ACE2-binding RBD design. We relied on the crystal structure of the spike protein receptor-binding domain from a SARS coronavirus designed human strain complexed with the human receptor ACE2 (PDB 3SCI, resolution 2.9Å) as a template for comparative modeling.	./cache/cord-328189-jpkxjn6e.txt	./txt/cord-328189-jpkxjn6e.txt