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Article

Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes.

Molecular cell - 9 Mar 2007

Schlieker Christian, Weihofen Wilhelm A, Frijns Evelyne, Kattenhorn Lisa M, Gaudet Rachelle, Ploegh Hidde L

Abstract excerpt

All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 17349955
DOI: 10.1016/j.molcel.2007.01.033
PMCID: PMC7110467

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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