id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-273893-3nd6ptrg	Lu, Guangwen	Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26	2013-07-07		.txt	text/plain	4674	260	56	Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition.	./cache/cord-273893-3nd6ptrg.txt	./txt/cord-273893-3nd6ptrg.txt