| In order to get insight into the structure characteristics of nonstructural protein NS3 and potential small molecular drugs against human Norovirus, series of bioinformatics websites and databases: ProtParam, ProtScale, SignalP 5.0, TMHMM 2.0, NCBI Conserved Domains, SOPMA, SWISS-MODEL, YinOYang 1.2, NetPhos 3.1, ABCpred, SYFPEITHI, Prankweb and Discovery Studio were used to analyze sequence identity, physicochemical properties, post-translational modification sites, secondary/tertiary structures, B/T cells epitopes, binding pockets and small molecule inhibitory compounds. The nonstructural protein NS3 is a stable hydrophilic protein composed of 363 amino acids with a relative molecular weight of 39 748.79 Da with theoretical isoelectric point at 6.37. The sequence identity between the NS3 and other virus helicases is 32.52%. The secondary structure mainly is α-helix and random coil, and it lacks a signal peptide and transmembrane region, with 2 functional domains, possessing 38 O-glycosylation sites, 21 phosphorylation sites, and 7 B-cell epitopes, 19 T-cell epitopes, 6 possible active binding pockets, 5 potential small molecule compounds. To summarize, this paper would provide theoretical foundation for understanding the structure information and mechanisms of nonstructural protein NS3 in acute viral gastroenteritis. Furthermore, it offers a basis for the development and screening antiviral drugs and vaccines targeting the NS3 of human norovirus. |
