2WK6

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

2WK6 の概要

• エントリーDOI: 10.2210/pdb2wk6/pdb
• 関連するPDBエントリー: 1UOU 2J0F 2WK5
• 分子名称: THYMIDINE PHOSPHORYLASE, 5-IODOURACIL (3 entities in total)
• 機能のキーワード: glycosyltransferase, developmental protein, angiogenesis, 5-iodouracil, growth factor, enzyme kinetics, differentiation, disease mutation, thymidine phosphorylase, chemotaxis, transferase, mutagenesis, polymorphism
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 100484.57

構造登録者

Mitsiki, E.,Papageorgiou, A.C.,Iyer, S.,Thiyagarajan, N.,Prior, S.H.,Sleep, D.,Finnis, C.,Acharya, K.R. (登録日: 2009-06-05, 公開日: 2009-07-07, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)