Structures of native human thymidine phosphorylase and in complex with 5-iodouracil
Copyright policy )Structures of native human thymidine phosphorylase and in complex with 5-iodouracil
Thymidine phosphorylase (TP) first identified as platelet derived endothelial cell growth factor (PD-ECGF) plays a key role in nucleoside metabolism. Human TP (hTP) is implicated in angiogenesis and is overexpressed in several solid tumors. Here, we report the crystal structures of recombinant hTP and its complex with a substrate 5-iodouracil (5IUR) at 3.0 and 2.5A, respectively. In addition, we provide information on the role of specific residues in the enzymatic activity of hTP through mutagenesis and kinetic studies.
- University Hospital Southampton NHS Foundation Trust United Kingdom
- University of Bath United Kingdom
- University Of Bath
- University of Nottingham United Kingdom
- Southampton General Hospital United Kingdom
Thymidine phosphorylase, Thymidine Phosphorylase, Protein Conformation, Crystal structure, Enzyme kinetics, Biophysics, Cell Biology, Crystallography, X-Ray, Biochemistry, Article, Phosphates, Mutagenesis, Mutation, Humans, 5-Iodouracil, Uracil, Molecular Biology
Thymidine phosphorylase, Thymidine Phosphorylase, Protein Conformation, Crystal structure, Enzyme kinetics, Biophysics, Cell Biology, Crystallography, X-Ray, Biochemistry, Article, Phosphates, Mutagenesis, Mutation, Humans, 5-Iodouracil, Uracil, Molecular Biology
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