Exploring structure-activity relationships of transition state analogues of human purine nucleoside phosphorylase.
Article Details
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Evans GB, Furneaux RH, Lewandowicz A, Schramm VL, Tyler PC
Exploring structure-activity relationships of transition state analogues of human purine nucleoside phosphorylase.
J Med Chem. 2003 Jul 17;46(15):3412-23.
- PubMed ID
- 12852771 [ View in PubMed]
- Abstract
The aza-C-nucleosides, Immucillin-H and Immucillin-G, are transition state analogue inhibitors of purine nucleoside phosphorylase, a therapeutic target for the control of T-cell proliferation. Immucillin analogues modified at the 2'-, 3'-, or 5'-positions of the azasugar moiety or at the 6-, 7-, or 8-positions of the deazapurine, as well as methylene-bridged analogues, have been synthesized and tested for their inhibition of human purine nucleoside phosphorylase. All analogues were poorer inhibitors, which reflects the superior capture of transition state features in the parent immucillins.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Forodesine Purine nucleoside phosphorylase Ki (nM) 3.3 N/A N/A Details Forodesine Purine nucleoside phosphorylase Ki (nM) 0.056 N/A N/A Details Immucillin-G Purine nucleoside phosphorylase Ki (nM) 0.54 N/A N/A Details Immucillin-G Purine nucleoside phosphorylase Ki (nM) 0.042 N/A N/A Details