Isaksson Johan, Woestenenk Esmeralda, Sahlberg Christer, Agback Tatiana
Drug Discovery and Design, Department of Chemistry, University of Tromsø, N-9037, Tromsø, Norway,
Biomol NMR Assign. 2014 Apr;8(1):81-4. doi: 10.1007/s12104-013-9457-7. Epub 2013 Jan 11.
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.
核相关脱氧尿苷5'-三磷酸核苷酸水解酶（dUTPase）是一种将脱氧尿苷5'-三磷酸（dUTP）水解为单磷酸的酶，从而控制生物体的dUTP水平，这对生存至关重要。此外，dUTPase在许多癌症中上调。因此，dUTPase是一个极具吸引力的潜在药物靶点。我们首次报告了由3×164个氨基酸组成的人源dUTPase同三聚体的近乎完整的核磁共振（NMR）光谱（15）N/（13）C/（1）H主链归属。此前，dUTPase家族中任何一种蛋白质仅发表了少数属于柔性C末端的主链共振信息。
