TAILIEUCHUNG - Báo cáo khoa học: Comparison of the substrate specificity of two potyvirus proteases

The substrate specificity of the nuclear inclusion protein a (NIa) proteolytic enzymes from two potyviruses, the tobacco etch virus (TEV) and tobacco vein mottling virus (TVMV), was compared using oligopeptide substrates. Mutations were introduced into TEV protease in an effort to identify key determinants of substrate specificity. The specificity of the mutant enzymes was assessed by using peptides with complementary substitutions. The crys-tal structure of TEV protease and a homology model of TVMV protease were used to interpret the kinetic data | iFEBS Journal Comparison of the substrate specificity of two potyvirus proteases A7Qof TAĩcór1 Inconh p Tkhhoq2 55r o ChortT 2 Potot Ranncci1 Tortr ri f oriolanH3 Juzoci I Uzoci JUocpii c. I loped SUUU Ciieiiy rctcMjayuos icily Ư. copeiaiiu Alexander Wlodawer2 and David S. Waugh2 1 Department of Biochemistry and Molecular Biology Research Center for Molecular Medicine University of Debrecen Hungary 2 Macromolecular Crystallography Laboratory Center for Cancer Research NationalCancer Institute at Frederick MD USA 3 Laboratory of Protein Dynamics and Signaling Center for Cancer Research NationalCancer Institute at Frederick MD USA Keywords nuclear inclusion protease potyvirus protease substrate specificity tobacco etch virus protease tobacco vein mottling virus protease Correspondence J. Tozser Department of Biochemistry and Molecular Biology Research Center for Molecular Medicine University of Debrecen Debrecen Hungary Fax 1 36 52 314 989 Tel 1 36 52 416 432 E-mail tozser@ or D. S. Waugh Macromolecular Crystallography Laboratory Center for Cancer Research NationalCancer Institute at Frederick PO Box B Frederick MD USA Fax 301 846 7148 Tel 301 846 1842 E-mail waughd@ The substrate specificity of the nuclear inclusion protein a NIa proteolytic enzymes from two potyviruses the tobacco etch virus TEV and tobacco vein mottling virus TVMV was compared using oligopeptide substrates. Mutations were introduced into TEV protease in an effort to identify key determinants of substrate specificity. The specificity of the mutant enzymes was assessed by using peptides with complementary substitutions. The crystal structure of TEV protease and a homology model of TVMV protease were used to interpret the kinetic data. A comparison of the two structures and the experimental data suggested that the differences in the specificity of the two enzymes may be mainly due to the variation in their S4 and S3 binding subsites. Two key residues predicted to be .

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