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Action at the assemblin dimer interface

Nature Structural Biology volume 8, pages 739741 (2001) | Download Citation

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A recent study of cytomegalovirus assemblin proteinase suggests that dimer-induced stabilization of the oxyanion hole may activate the enzyme.

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Affiliations

  1. Wade Gibson is at The Johns Hopkins School of Medicine, Pharmaclogy & Molecular Sciences, 725 N. Wolfe Street, Baltimore, Maryland 21205 USA. wgibson@jhmi.edu

    • Wade Gibson

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DOI

https://doi.org/10.1038/nsb0901-739

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