SARS is a positive-stranded virus featuring the largest viral RNA genomes today. The viral main proteinase(Hydrolase), controlling the activities of SARS virus replication , is an attractive target for therapy. We det...SARS is a positive-stranded virus featuring the largest viral RNA genomes today. The viral main proteinase(Hydrolase), controlling the activities of SARS virus replication , is an attractive target for therapy. We determined crystal structure for transmissible gastroenteritis virus(TGEV) hydrolase, and constructed a homology model for SARS coronavirus proteinase on Silicon Graphics station by Insight Ⅱ molecule simulation software. The structure may reveal remarkable degree of conservation of the substrate binding sites. We design an imaginable peptide precursor for inhibitor, and the base shape of pocket and property of the residues may be used as a basis for designing anti-SARS drugs.展开更多
With a view to finding out precisely how small peptides recognize a particular binding site of DNA, we have accomplished DNA binding studies of two peptides, H-Tyr-Arg-OH (YR) and H-Gly-Gly-His-OH (GGH) by using measu...With a view to finding out precisely how small peptides recognize a particular binding site of DNA, we have accomplished DNA binding studies of two peptides, H-Tyr-Arg-OH (YR) and H-Gly-Gly-His-OH (GGH) by using measurements in comparison with the binding between DNA and Hoechst 33258. The inhibition mode by YR and GGH to DNA binding of Hoechst 33258 was analyzed by Lineweaver-Burk plot which shows the plot of typical competitive inhibition at concentration of Hoechst 33258 from 3.66 ( 10-9 mol / L to 1.09 ( 10-8 mol / L. And it is concluded that YR binds to DNA in its minor groove (AT rich regions) with a binding constant K = 1.02 ( 108 (mol / L)-1. The GGH(s specificity is reduced at high concentration because it can also bind GC base pair.展开更多
文摘SARS is a positive-stranded virus featuring the largest viral RNA genomes today. The viral main proteinase(Hydrolase), controlling the activities of SARS virus replication , is an attractive target for therapy. We determined crystal structure for transmissible gastroenteritis virus(TGEV) hydrolase, and constructed a homology model for SARS coronavirus proteinase on Silicon Graphics station by Insight Ⅱ molecule simulation software. The structure may reveal remarkable degree of conservation of the substrate binding sites. We design an imaginable peptide precursor for inhibitor, and the base shape of pocket and property of the residues may be used as a basis for designing anti-SARS drugs.
文摘With a view to finding out precisely how small peptides recognize a particular binding site of DNA, we have accomplished DNA binding studies of two peptides, H-Tyr-Arg-OH (YR) and H-Gly-Gly-His-OH (GGH) by using measurements in comparison with the binding between DNA and Hoechst 33258. The inhibition mode by YR and GGH to DNA binding of Hoechst 33258 was analyzed by Lineweaver-Burk plot which shows the plot of typical competitive inhibition at concentration of Hoechst 33258 from 3.66 ( 10-9 mol / L to 1.09 ( 10-8 mol / L. And it is concluded that YR binds to DNA in its minor groove (AT rich regions) with a binding constant K = 1.02 ( 108 (mol / L)-1. The GGH(s specificity is reduced at high concentration because it can also bind GC base pair.
