title: Backbone nuclear magnetic resonance assignment of human deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase).
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 (15)N/(13)C/(1)H 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.
authors: Drug Discovery and Design, Department of Chemistry, University of Tromsø, N-9037, Tromsø, Norway, johan.isaksson@uit.no.
authors: Johan
authors: J
authors: Isaksson
authors: Esmeralda
authors: E
authors: Woestenenk
authors: Christer
authors: C
authors: Sahlberg
authors: Tatiana
authors: T
authors: Agback
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D011755:Pyrophosphatases / Q000737:chemistry*
chemical_list: D021122:Protein Subunits; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase