L-Enantiomers of Transition State Analogue Inhibitors Bound to Human Purine Nucleoside Phosphorylase

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• 作者：Agnes Rinaldo-Matthis ; Andrew S. Murkin ; Udupi A. Ramagopal ; Keith Clinch ; Simon P. H. Mee ; Gary B. Evans ; Peter C. Tyler ; Richard H. Furneaux ; Steven C. Almo ; Vern L. Schramm
• 刊名：Journal of the American Chemical Society
• 出版年：2008
• 出版时间：January 23, 2008
• 年：2008
• 卷：130
• 期：3
• 页码：842 - 844
• 全文大小：221K
• 年卷期：v.130,no.3(January 23, 2008)
• ISSN：1520-5126

文摘

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.