id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-298482-r7lallv0	De Maio, Flavio	Improved binding of SARS-CoV-2 Envelope protein to tight junction-associated PALS1 could play a key role in COVID-19 pathogenesis	2020-09-04		.txt	text/plain	1739	86	54	title: Improved binding of SARS-CoV-2 Envelope protein to tight junction-associated PALS1 could play a key role in COVID-19 pathogenesis When compared to the known SARS E protein, we observed a significant difference in amino acid sequence in the C-terminal end of SARS-CoV-2 E protein. The amino acid sequence of the SARS-CoV-2 Envelope protein was extracted, and the NMR structure of the 119 homologous protein of SARS-CoV (PDB code: 2MM4) was used as a template. In Figure 1B and 1C, the two predicted monomeric E full length protein structure models have been 159 constructed and show N-terminal (blue), transmembrane (green), C-terminal domains (red) as well as the 160 amino acid variants (yellow). In order to verify the potential implications of the altered amino acid sequence, the binding pose of the two 174 C-terminus octapeptides belonging to SARS-CoV and SARS-CoV-2 were determined and compared with 175 the crystallographic structure of the complex PALS1-CRB1[31].	./cache/cord-298482-r7lallv0.txt	./txt/cord-298482-r7lallv0.txt