Journal Title
Title of Journal: Biomol NMR Assign
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Abbravation: Biomolecular NMR Assignments
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Publisher
Springer Netherlands
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Authors: Johan Isaksson Esmeralda Woestenenk Christer Sahlberg Tatiana Agback
Publish Date: 2013/01/11
Volume: 8, Issue: 1, Pages: 81-84
Abstract
Nuclearassociated 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 upregulated 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 homotrimer human dUTPase Previously only a handful backbone resonances belonging to the flexible Cterminus has been published for any protein in the dUTPase family
Keywords:
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Other Papers In This Journal:
- Letter to the Editor: Resonance assignment of SlyD from E. coli
- NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1
- A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216)
- 1 H, 13 C, 15 N resonance assignment of the chitin-binding protein CBP21 from Serratia marcescens
- 1 H, 13 C, and 15 N assignment of the muscular LIM protein MLP/CRP3
- Backbone and sidechain 1 H, 13 C and 15 N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid
- 1 H, 13 C and 15 N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis
- 1 H, 13 C, 15 N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the Hv GR-RBP1 protein involved in the regulation of barley ( Hordeum vulgare L.) senescence
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