3EUF

Crystal structure of BAU-bound human uridine phosphorylase 1

3EUF の概要

• エントリーDOI: 10.2210/pdb3euf/pdb
• 関連するPDBエントリー: 3EUE
• 分子名称: Uridine phosphorylase 1, 1-((2-HYDROXYETHOXY)METHYL)-5-BENZYLPYRIMIDINE-2,4(1H,3H)-DIONE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: nucleoside phosphorylase, uridine rescue, 5-benzylacyclouridine, alternative splicing, glycosyltransferase, transferase
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145687.50

構造登録者

Roosild, T.P. (登録日: 2008-10-10, 公開日: 2009-03-31, 最終更新日: 2023-09-06)

主引用文献

Roosild, T.P.,Castronovo, S.,Fabbiani, M.,Pizzorno, G.
Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy.
Bmc Struct.Biol., 9:14-14, 2009

PubMed Abstract: Uridine phosphorylase (UPP) is a key enzyme of pyrimidine salvage pathways, catalyzing the reversible phosphorolysis of ribosides of uracil to nucleobases and ribose 1-phosphate. It is also a critical enzyme in the activation of pyrimidine-based chemotherapeutic compounds such a 5-fluorouracil (5-FU) and its prodrug capecitabine. Additionally, an elevated level of this enzyme in certain tumours is believed to contribute to the selectivity of such drugs. However, the clinical effectiveness of these fluoropyrimidine antimetabolites is hampered by their toxicity to normal tissue. In response to this limitation, specific inhibitors of UPP, such as 5-benzylacyclouridine (BAU), have been developed and investigated for their ability to modulate the cytotoxic side effects of 5-FU and its derivatives, so as to increase the therapeutic index of these agents.

PubMed: 19291308
DOI: 10.1186/1472-6807-9-14

実験手法

X-RAY DIFFRACTION (1.9 Å)