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

概要

論文の詳細を見る
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 α 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.
日本生物物理学会の論文
2006-03-25