id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-030654-8yxa1r1c	Zhang, Changhui	Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2	2020-08-20		.txt	text/plain	4281	289	62	This structure was revealed to be a horseshoe-like tetramer, which may play an essential role in nsp9 oligomerization and in the regulation of viral nucleic acid binding during the replication of the virus. The initial structure solved by molecular replacement showed that six SARS-CoV-2 nsp9 protomers form an OB-fold cluster in an asymmetric unit ( Supplementary Fig. 1a ). To obtain more information about the protein interfaces and the likely biological assemblies of the OB-fold cluster, we calculated the structure of SARS-CoV-2 nsp9 using PDBe-PISA [27] . These three contact surfaces in interface I b/c contribute a hydrophobic base with eight hydrogen bonds and one salt bridge, making the SARS-CoV-2 nsp9 tetramer extremely stable in the crystal structure. In this present study, we observed the nucleic acid-binding ability of SARS-CoV-2 nsp9, using the electrophoretic mobility The molecules in these two interfaces are shown as cartoons and colored and labeled as in Fig. 2a .	./cache/cord-030654-8yxa1r1c.txt	./txt/cord-030654-8yxa1r1c.txt