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  • Title: L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.
    Author: Rinaldo-Matthis A, Murkin AS, Ramagopal UA, Clinch K, Mee SP, Evans GB, Tyler PC, Furneaux RH, Almo SC, Schramm VL.
    Journal: J Am Chem Soc; 2008 Jan 23; 130(3):842-4. PubMed ID: 18154341.
    Abstract:
    Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.
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