Rinaldo-Matthis Agnes, Murkin Andrew S, Ramagopal Udupi A, Clinch Keith, Mee Simon P H, Evans Gary B, Tyler Peter C, Furneaux Richard H, Almo Steven C, Schramm Vern L
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Am Chem Soc. 2008 Jan 23;130(3):842-4. doi: 10.1021/ja710733g. Epub 2007 Dec 23.
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.
人类嘌呤核苷磷酸化酶（PNP）与用L-立体化学的核糖基模拟物合成的过渡态类似物抑制剂Immucillin-H和DADMe-Immucillin-H一起结晶。这些抑制剂表明，尽管与人类PNP结合的d-Immucillins和l-Immucillins发生了较大的几何变化，但这些类似物紧密结合的主要驱动力是离去基团相互作用和过渡态的阳离子模拟。
