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 a...

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Detalles Bibliográficos
Autores principales: Mitsiki, Eirini, Papageorgiou, Anastassios C., Iyer, Shalini, Thiyagarajan, Nethaji, Prior, Steven H., Sleep, Darrell, Finnis, Chris, Acharya, K. Ravi
Formato: Texto
Lenguaje:English
Publicado: Academic Press 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2719695/
https://www.ncbi.nlm.nih.gov/pubmed/19555658
http://dx.doi.org/10.1016/j.bbrc.2009.06.104
Descripción
Sumario: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 2.5 Å, respectively. In addition, we provide information on the role of specific residues in the enzymatic activity of hTP through mutagenesis and kinetic studies.

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