Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA 92093, USA.
Trends Biochem Sci. 2011 Feb;36(2):65-77. doi: 10.1016/j.tibs.2010.09.006. Epub 2010 Oct 23.
Eukayotic protein kinases evolved as a family of highly dynamic molecules with strictly organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for assembly of the entire molecule. Two non-consecutive hydrophobic structures termed "spines" anchor all the elements important for catalysis to the F-helix. They make firm, but flexible, connections within the molecule, providing a high level of internal dynamics of the protein kinase. During the course of evolution, protein kinases developed a universal regulatory mechanism associated with a large activation segment that can be dynamically folded and unfolded in the course of cell functioning. Protein kinases thus represent a unique, highly dynamic, and precisely regulated set of switches that control most biological events in eukaryotic cells.
真核生物蛋白激酶作为一个高度动态的分子家族而进化，其内部结构严格有序。一个单一的疏水性 F 螺旋作为整个分子组装的中央支架。两个不连续的疏水性结构称为“刺”，将所有对催化至关重要的元件锚定在 F 螺旋上。它们在分子内部建立牢固但灵活的连接，提供蛋白激酶的高度内部动力学。在进化过程中，蛋白激酶形成了与大激活片段相关的通用调节机制，该激活片段在细胞功能过程中可以动态折叠和展开。因此，蛋白激酶代表了一组独特的、高度动态的、精确调节的开关，控制真核细胞中的大多数生物事件。
