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Action at the assemblin dimer interface

Nature Structural Biology volume 8, pages 739–741 (2001)Cite this article

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

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Figure 1: CMV assemblin is derived from a precursor.
Figure 2: CMV proteinase is essential during capsid maturation.

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  1. The Johns Hopkins School of Medicine, Pharmaclogy & Molecular Sciences, 725 N. Wolfe Street, Baltimore, Maryland, 21205, USA

    Wade Gibson

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Gibson, W. Action at the assemblin dimer interface. Nat Struct Mol Biol 8, 739–741 (2001). https://doi.org/10.1038/nsb0901-739

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