RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Org Biomol Chem. 2012 Apr 7;10(13):2607-12. doi: 10.1039/c2ob06636j. Epub 2012 Feb 27.
One useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-β-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-β-N-acetylhexosaminidases but also other types of glycoside hydrolases.
一种有用的方法是通过晶体学研究抑制剂-酶复合物，深入了解化学合成抑制剂与酶结合的方式以及它们具有高效性的原因。本文呈现了一类具有代表性的 20 家族外切-β-N-乙酰己糖苷酶与各种已知抑制剂类别的复合物的 X 射线结构分析，该分析突出了不同抑制剂类别如何抑制相同的酶。这项研究不仅有助于外切-β-N-乙酰己糖苷酶抑制剂的进一步开发，也有助于其他类型糖苷水解酶抑制剂的开发。
