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Protease dimer formation disrupted

Nature Chemical Biology volume 5, pages 607–608 (2009)Cite this article

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.

Interactions between two or more proteins have profound implications for a wide range of biological processes—from complex cellular signaling to, in the case of the article by Shahian et al.1, the assembly of viral proteins into functional enzymes. Science has seen an avalanche of information on the biological consequences of protein interactions both in homeostasis and disease, and a rich literature is emerging on the structural motifs found at protein interfaces. Although the field is growing, efforts to modulate these interactions—a feat that would be quite useful for treating disease states—are truly in their infancy2,3.

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References

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  1. Jean Chmielewski is in the Department of Chemistry, Purdue University, West Lafayette, Indiana, USA. chml@purdue.edu,

    Jean Chmielewski

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  1. Jean Chmielewski
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Chmielewski, J. Protease dimer formation disrupted. Nat Chem Biol 5, 607–608 (2009). https://doi.org/10.1038/nchembio0909-607

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  • DOI: https://doi.org/10.1038/nchembio0909-607

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