Structural highlights
Function
[PNPH_BOVIN] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The combined use of a rapid virtual screen of a small fragment library together with a single point enzyme assay has been used for the discovery of novel PNP inhibitors. The availability of readily soakable crystals of bovine PNP has allowed the approach to be experimentally validated by determining the crystal structure of one of the inhibitor-PNP complexes. Comparison of the experimentally determined binding mode with that predicted by the virtual screening shows them to be similar. This represents a starting point for the growth of the ligand into a higher affinity inhibitor.
Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue.,Pereira HM, Berdini V, Cleasby A, Garratt RC FEBS Lett. 2007 Oct 30;581(26):5082-6. Epub 2007 Oct 2. PMID:17927987[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pereira HM, Berdini V, Cleasby A, Garratt RC. Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue. FEBS Lett. 2007 Oct 30;581(26):5082-6. Epub 2007 Oct 2. PMID:17927987 doi:10.1016/j.febslet.2007.09.051
