Action at the assemblin dimer interface

W. Gibson

doi:10.1038/nsb0901-739

Action at the assemblin dimer interface

W. Gibson

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

4 Scopus citations

Abstract

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

Original language	English (US)
Pages (from-to)	739-741
Number of pages	3
Journal	Nature Structural Biology
Volume	8
Issue number	9
DOIs	https://doi.org/10.1038/nsb0901-739
State	Published - 2001

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "Action at the assemblin dimer interface",

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

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Action at the assemblin dimer interface

Abstract

ASJC Scopus subject areas

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