3EUE
Crystal structure of ligand-free human uridine phosphorylase 1 (hUPP1)
Summary for 3EUE
| Entry DOI | 10.2210/pdb3eue/pdb |
| Related | 3EUF |
| Descriptor | Uridine phosphorylase 1, MAGNESIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | nucleoside phosphorylase, uridine rescue, alternative splicing, glycosyltransferase, transferase |
| Biological source | Homo sapiens |
| Total number of polymer chains | 1 |
| Total formula weight | 36170.99 |
| Authors | Roosild, T.P. (deposition date: 2008-10-09, release date: 2009-03-31, Last modification date: 2023-09-06) |
| Primary citation | 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 Cited by 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: 19291308DOI: 10.1186/1472-6807-9-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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