Kenakin Terry P
Department of Biological Reagents and Assay Development, GlaxoSmithKline Research and Development, 5 Moore Drive, Research Triangle Park, NC 27709, USA.
Mol Pharmacol. 2008 Sep;74(3):541-3. doi: 10.1124/mol.108.050062. Epub 2008 Jun 26.
The article in this issue by Redka et al. (p. 834) illustrates some interesting interactions between classified orthosteric (bind to the same recognition site as endogenous agonist) and allosteric (bind to a different site) ligands. Of particular interest are the methods used to deal with an obfuscating factor in these kinds of studies, namely the propensity of seven transmembrane receptors to form dimers and thus demonstrate allosteric effects through binding at the orthosteric site. The judicious use of kinetics to detect and quantify allosteric action also is demonstrated. The various unique properties of allosteric modulators are discussed in the context of the increasing prevalence of allosteric ligands as investigational drugs.
本期由雷德卡等人撰写的文章（第834页）阐述了一些在分类的正构（与内源性激动剂结合于同一识别位点）和变构（结合于不同位点）配体之间有趣的相互作用。特别值得关注的是在这类研究中用于处理一个混淆因素的方法，即七跨膜受体形成二聚体并因此通过在正构位点结合而表现出变构效应的倾向。同时还展示了明智地运用动力学来检测和量化变构作用。在变构配体作为研究性药物的日益普及的背景下，讨论了变构调节剂的各种独特性质。
