Hauske Patrick, Ottmann Christian, Meltzer Michael, Ehrmann Michael, Kaiser Markus
Chemical Genomics Centre der Max-Planck-Gesellschaft, Dortmund, Germany.
Chembiochem. 2008 Dec 15;9(18):2920-8. doi: 10.1002/cbic.200800528.
Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors.
变构是基于蛋白质或小分子在与酶活性中心不同的位点相互作用来控制酶活性的基本原理。变构调节剂代表了一种设计和合成蛋白酶小分子激活剂或抑制剂的替代方法，因此在药物化学领域备受关注。一些蛋白质类和小分子变构蛋白酶调节剂的结构基础已经阐明，这表明了一种可能用于未来小分子效应物合理设计的通用机制。
