Biomolecular NMR Assignments

, Volume 8, Issue 1, pp 81–84 | Cite as

Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase)

  • Johan Isaksson
  • Esmeralda Woestenenk
  • Christer Sahlberg
  • Tatiana Agback
Article
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Accepted:

Abstract

Nuclear-associated deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase) is an enzyme that hydrolyses deoxyuridine 5′-triphosphate (dUTP) to the monophosphate, thereby controlling the dUTP levels of the organism, which is essential for survival. Further, dUTPase is up-regulated in many cancers. Thus, dUTPase is a highly interesting potential drug target. We report, for the first time, the near complete nuclear magnetic resonance (NMR) spectroscopy 15N/13C/1H backbone assignment of the 3 × 164 amino acids homo-trimer human dUTPase. Previously, only a handful backbone resonances belonging to the flexible C-terminus has been published for any protein in the dUTPase family.

Keywords

Human dUTPase Protein backbone assignment Multidimensional NMR 

Abbreviations

dUTP

Deoxyuridine 5′-triphosphate

dUTPase

Deoxyuridine 5′-triphosphate nucleotidohydrolase

NMR

Nuclear magnetic resonance

HSQC

Heteronuclear single quantum coherence

dUPNPP

2′-deoxyuridine 5′-α,β-imido-triphosphate

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Supplementary material

12104_2013_9457_MOESM1_ESM.doc (2.3 mb)
Supplementary material 1 (DOC 2327 kb)

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Johan Isaksson
    • 1
  • Esmeralda Woestenenk
    • 2
  • Christer Sahlberg
    • 2
  • Tatiana Agback
    • 2
  1. 1.Drug Discovery and Design, Department of ChemistryUniversity of TromsøTromsøNorway
  2. 2.Medivir AB22 HuddingeSweden

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