Protease dimer formation disrupted.
A small-molecule inhibitor of the obligate dimeric protease of human Kaposi's sarcoma-associated herpesvirus was identified. The agent functions by a "monomer trap" mechanism in which the compound binds to a partially unfolded monomer and disrupts the formation of the enzymatically active protease dimer.
Chmielewski
Jean
J
Department of Chemistry, Purdue University, West Lafayette, Indiana, USA. chml@purdue.edu
D019288:Herpesvirus 8, Human / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D017510:Protein Folding; D055503:Protein Multimerization / Q000187:drug effects*; D054852:Small Molecule Libraries
D011480:Protease Inhibitors; D054852:Small Molecule Libraries; D010447:Peptide Hydrolases
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