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Architecturally diverse proteins converge on an analogous mechanism to inactivate Uracil-DNA glycosylase

DOI: 10.1093/nar/gkt633 DOI Help
PMID: 23892286 PMID Help

Authors: Ambrose R. Cole (Birkbeck College, University of London) , Sapir Ofer (Birkbeck College, University of London; University College London) , Ksenia Ryzhenkova (Birkbeck College, University of London) , Gediminas Baltulionis (Birkbeck College, University of London) , P. Hornyak (Birkbeck College, University of London) , Renos Savva (Birkbeck College, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research

State: Published (Approved)
Published: July 2013

Open Access Open Access

Abstract: Uracil-DNA glycosylase (UDG) compromises the replication strategies of diverse viruses from unrelated lineages. Virally encoded proteins therefore exist to limit, inhibit or target UDG activity for proteolysis. Viral proteins targeting UDG, such as the bacteriophage proteins ugi, and p56, and the HIV-1 protein Vpr, share no sequence similarity, and are not structurally homologous. Such diversity has hindered identification of known or expected UDG-inhibitory activities in other genomes.

Journal Keywords: Bacillus; Binding; Catalytic; DNA; Herpesvirus; Human; Humans; Hydrophobic; Leucine; Models; Molecular;Mutation; Protein; Secondary; Uracil-DNA; Viral Proteins

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 31/07/2013 21:18

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