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Structures of native human thymidine phosphorylase and in complex with 5-iodouracil.

Mitsiki, E; Papageorgiou, AC; Iyer, S; Thiyagarajan, N; Prior, SH; Sleep, D; Finnis, C; (2009) Structures of native human thymidine phosphorylase and in complex with 5-iodouracil. Biochem Biophys Res Commun , 386 (4) pp. 666-670. 10.1016/j.bbrc.2009.06.104.

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Abstract

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.

Type: Article
Title: Structures of native human thymidine phosphorylase and in complex with 5-iodouracil.
Location: United States
DOI: 10.1016/j.bbrc.2009.06.104
Keywords: Crystallography, X-Ray, Humans, Mutation, Phosphates, Protein Conformation, Thymidine Phosphorylase, Uracil
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1486310
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