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Recombinant, bacterially expressed apoptin protein inducesapoptosis inhuman tumour cell lines but not innormal cells,mimicking the behaviour of ectopically expressed apoptin.Recombinant apoptin is isolated exclusively as a highlystablemultimeric complex of 30–40monomers, with little, ifany,a-helical and b-sheet structure. Despite its apparentdisorder, multimeric apoptin is biologically active. Here, wepresent evidence thatmost of the apoptinmoietieswithin thecomplex may well share a similar conformation. Further-more, the multimer has extensive and uniformhydrophobicpatches and conformationally stable domains. ...
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Báo cáo khoa học: Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer
