Regulating the Activity of the Herpesviral Protease and Its Viable Target for Inhibition

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  • ヘルペスウイルスプロテアーゼの活性制御機構と新たな阻害部位
  • ヘルペスウイルスプロテアーゼ ノ カッセイ セイギョ キコウ ト アラタ ナ ソガイ ブイ

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Abstract

Kaposi’s sarcoma-associated herpesvirus (KSHV), like all herpesviruses, encodes a protease (KSHV Pr), which is necessary for the viral lytic cycle. Herpesviral proteases function as obligate dimers, however, each monomer has an active site, which is spatially separate from the dimer interface. To address the potential of targeting the dimer interface, a 30 amino acid helical peptide was synthesized by protein grafting of an interfacial KSHV Pr a helix with a small stable protein, avian pancreatic polypeptide (aPP) to disrupt the dimerization of KSHV Pr. Biochemical analysis revealed that the rationally designed helical peptide inhibited KSHV Pr dimerization and activity. These results indicate that the dimer interface, as well as the active sites, of herpesvirus proteases is a viable target for inhibiting enzyme activity.<br>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 46 (2), 87-92, 2006

    The Biophysical Society of Japan General Incorporated Association

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