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


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.

SUBMITTER: Mitsiki E 

PROVIDER: S-EPMC2719695 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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

Mitsiki Eirini E   Papageorgiou Anastassios C AC   Iyer Shalini S   Thiyagarajan Nethaji N   Prior Steven H SH   Sleep Darrell D   Finnis Chris C   Acharya K Ravi KR  

Biochemical and biophysical research communications 20090623 4


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 mutagen  ...[more]

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