Reményi Attila, Good Matthew C, Lim Wendell A
Department of Cellular and Molecular Pharmacology, Program in Biological Sciences, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.
Curr Opin Struct Biol. 2006 Dec;16(6):676-85. doi: 10.1016/j.sbi.2006.10.008. Epub 2006 Oct 31.
To achieve high biological specificity, protein kinases and phosphatases often recognize their targets through interactions that occur outside of the active site. Although the role of modular protein-protein interaction domains in kinase and phosphatase signaling has been well characterized, it is becoming clear that many kinases and phosphatases utilize docking interactions - recognition of a short peptide motif in target partners by a groove on the catalytic domain that is separate from the active site. Docking is particularly prevalent in serine/threonine kinases and phosphatases, and is a versatile organizational tool for building complex signaling networks; it confers a high degree of specificity and, in some cases, allosteric regulation.
为实现高生物学特异性，蛋白激酶和磷酸酶通常通过活性位点之外发生的相互作用来识别其靶标。尽管模块化蛋白-蛋白相互作用结构域在激酶和磷酸酶信号传导中的作用已得到充分表征，但越来越明显的是，许多激酶和磷酸酶利用对接相互作用——催化结构域上与活性位点分开的凹槽识别靶标伙伴中的短肽基序。对接在丝氨酸/苏氨酸激酶和磷酸酶中尤为普遍，是构建复杂信号网络的一种通用组织工具；它赋予高度特异性，在某些情况下还具有变构调节作用。
