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.
This is a preview of subscription content, access via your institution
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Rent or buy this article
Prices vary by article type
Prices may be subject to local taxes which are calculated during checkout
Shahian, T. et al. Nat. Chem. Biol. 5, 640–646 (2009).
Hershberger, S.J., Lee, S.G. & Chmielewski, J. Curr. Top. Med. Chem. 7, 928–942 (2007).
Wells, J.A. & McClendon, C.L. Nature 450, 1001–1009 (2007).
Jones, S. & Thornton, J.M. Proc. Natl. Acad. Sci. USA 93, 13–20 (1996).
Reiling, K.K., Pray, T.R., Craik, C.S. & Stroud, R.M. Biochemistry 39, 12796–12803 (2000).
Wu, T.D. et al. J. Virol. 77, 4836–4847 (2003).
About this article
Cite this article
Chmielewski, J. Protease dimer formation disrupted. Nat Chem Biol 5, 607–608 (2009). https://doi.org/10.1038/nchembio0909-607