Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

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

Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

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

Loading next page...
 
/lp/springer-journals/backbone-nuclear-magnetic-resonance-assignment-of-human-deoxyuridine-5-ppjM0pbbQ2
Publisher
Springer Journals
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-013-9457-7
pmid
23307478
Publisher site
See Article on Publisher Site

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.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jan 11, 2013

References