id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-300322-koqm5yxq	Li, Fang	Interactions Between Sars Coronavirus and its Receptor	2006		.txt	text/plain	1711	103	60	The SARS-CoV RBD is sufficient for tight binding to ACE2, and thus it is the most important determinant of virus-receptor interactions, viral host range, and tropism. 8 The final model of the complex contains the N-terminal peptidase domain of human ACE2 (residues 19-615) and the spike RBD of human SARS-CoV (residues 323-502, missing residues 376-381). The structure reveals important residue changes at the binding interface that determine the species specificity of SARS-CoV. 6, 7 Detailed structural analysis sheds light on the significance of these residues in virus-receptor interactions (Figure 4 ). Rat ACE2 does not support SARS-CoV Leu472 on the RBD has a hydrophobic interaction with Met82 on ACE2. On rat ACE2, residue 82 is glycosylated, preventing the binding of SARS-CoV. In summary, the crystal structure of SARS-CoV spike RBD in complex with ACE2 has revealed detailed interactions between the virus and its receptor. Structure of SARS coronavirus spike receptor-binding	./cache/cord-300322-koqm5yxq.txt	./txt/cord-300322-koqm5yxq.txt