2WK6

Structural features of native human thymidine phosphorylase and in complex with 5-iodouracil

Summary for 2WK6

• Entry DOI: 10.2210/pdb2wk6/pdb
• Related: 1UOU 2J0F 2WK5
• Descriptor: THYMIDINE PHOSPHORYLASE, 5-IODOURACIL (3 entities in total)
• Functional Keywords: glycosyltransferase, developmental protein, angiogenesis, 5-iodouracil, growth factor, enzyme kinetics, differentiation, disease mutation, thymidine phosphorylase, chemotaxis, transferase, mutagenesis, polymorphism
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 100484.57

Authors

Mitsiki, E.,Papageorgiou, A.C.,Iyer, S.,Thiyagarajan, N.,Prior, S.H.,Sleep, D.,Finnis, C.,Acharya, K.R. (deposition date: 2009-06-05, release date: 2009-07-07, Last modification date: 2023-12-13)

Primary citation

Mitsiki, E.,Papageorgiou, A.C.,Iyer, S.,Thiyagarajan, N.,Prior, S.H.,Sleep, D.,Finnis, C.,Acharya, K.R.
Structures of Native Human Thymidine Phosphorylase and in Complex with 5-Iodouracil.
Biochem.Biophys.Res.Commun., 386:666-, 2009

PubMed 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.

PubMed: 19555658
DOI: 10.1016/J.BBRC.2009.06.104

Experimental method

X-RAY DIFFRACTION (2.5 Å)