id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-323324-h2a25xym	Armijos‐Jaramillo, Vinicio	SARS‐CoV‐2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability	2020-05-07		.txt	text/plain	3340	192	55	With this analysis, we determine a region inside the receptor‐binding domain with putative sites under positive selection interspersed among highly conserved sites, which are implicated in structural stability of the viral spike protein and its union with human receptor ACE2. In the case of SARS-CoV, ACE2 binding was found to be a critical determinant for the range of hosts the virus can infect, and key amino acid residues in the RBD were identified to be essential for ACE2-mediated SARS-CoV infection and adaptation to humans (Li et al., 2005 (Li et al., , 2006 . We employ a multidisciplinary approach to look for evidence of diversifying selection on the S-protein gene and model the interactions between human ACE2 (hACE2) and the RBD of selected coronavirus strains, which ultimately afforded us novel insights detailing virus and host cell interactions. Additionally, important hACE2-binding residues in the RBD from SARS-COV-2 obtained from the crystallography and structure determination performed by Shang et al.	./cache/cord-323324-h2a25xym.txt	./txt/cord-323324-h2a25xym.txt