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• W2070141004 abstract "The summer leaf isoform of the pokeweed (Phytolacca americana) antiviral protein, PAP II, was produced in high yields from inclusion bodies in recombinantE. coli.On the basis of its sequence similarity with the spring leaf isoform (PAP I) and with the A chain of ricin, a three-dimensional model of the protein was constructed as an aid in the design of active-site mutants. PAP II variants mutated in residues Asp 88 (D88N), Tyr 117 (Y117S), Glu 172 (E172Q), Arg 175 (R175H) and a combination of Asp 88 and Arg 175 (D88N/R175H) were produced inE. coliand assayed for their ability to inhibit protein synthesis in a rabbit reticulocyte lysate. All of these mutations had effects deleterious to the enzymatic activity of PAP II. The results were interpreted in the light of three reaction mechanisms proposed for ribosome-inactivating proteins (RIPs). We conclude that none of the proposed mechanisms is entirely consistent with the data presented here." @default.
• W2070141004 created "2016-06-24" @default.
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• W2070141004 date "1998-12-01" @default.
• W2070141004 modified "2023-09-26" @default.
• W2070141004 title "Analysis of Active Site Residues of the Antiviral Protein from Summer Leaves fromPhytolacca americanaby Site-Directed Mutagenesis" @default.
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• W2070141004 doi "https://doi.org/10.1006/bbrc.1998.9815" @default.
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