Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 A resolution (R(cryst) = 17.6%, R(free) = 20.6%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.
The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution.,Lashkov AA, Zhukhlistova NE, Gabdoulkhakov AH, Shtil AA, Efremov RG, Betzel C, Mikhailov AM Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):51-60. Epub 2009, Dec 21. PMID:20057049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lashkov AA, Zhukhlistova NE, Gabdoulkhakov AH, Shtil AA, Efremov RG, Betzel C, Mikhailov AM. The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):51-60. Epub 2009, Dec 21. PMID:20057049 doi:10.1107/S0907444909044175
