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 N-15/C-13/H-1 backbone assignment of the 3 x 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

Published in

Biomolecular NMR Assignments
2014, Volume: 8, number: 1, pages: 81-84
Publisher: SPRINGER

UKÄ Subject classification

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


Publication identifier

DOI: https://doi.org/10.1007/s12104-013-9457-7

Permanent link to this page (URI)

https://res.slu.se/id/publ/99458