title: 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.
authors: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
authors: Eirini
authors: E
authors: Mitsiki
authors: Anastassios C
authors: AC
authors: Papageorgiou
authors: Shalini
authors: S
authors: Iyer
authors: Nethaji
authors: N
authors: Thiyagarajan
authors: Steven H
authors: SH
authors: Prior
authors: Darrell
authors: D
authors: Sleep
authors: Chris
authors: C
authors: Finnis
authors: K Ravi
authors: KR
authors: Acharya
mesh_terms: D018360:Crystallography, X-Ray; D006801:Humans; D009154:Mutation; D010710:Phosphates / Q000737:chemistry; D011487:Protein Conformation; D013939:Thymidine Phosphorylase / Q000737:chemistry* / Q000235:genetics; D014498:Uracil / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D010710:Phosphates; D014498:Uracil; D013939:Thymidine Phosphorylase; C048747:5-iodouracil