CRYSTALLOGRAPHIC ANALYSIS OF MAP KINASES

描述：这项研究项目的长期目标是了解 MAP激酶ERK2的复杂调控机制。贴图激酶是 荷尔蒙启动的信号转导途径的重要元素， 细胞因子，或环境压力。激活了诸如ERK2之类的MAP激酶 在被MAP/ERK激酶(MEK)磷酸化后，MEK本身就是 在细胞刺激后被Ras/Raf蛋白激活。因此，这些 酶可能是有用的治疗靶点。贴图激酶有几个 有趣的特性，包括复杂的双重磷酸化调节 机制和高底物专一性的羟基氨基酸是 然后是目标蛋白序列中的脯氨酸。极少的蛋白激酶 对系统进行了彻底的研究，没有一个系统有结晶学数据 对于同一种酶的非活性和活性或磷酸化形式。

DESCRIPTION: The long-term goal of this research project is to understand the complex regulatory mechanism of ERK2, a MAP kinase. MAP kinases are important elements of signal transduction pathways initiated by hormones, cytokines, or environmental stress. MAP kinases such as ERK2 are activated after phosphorylation by MAP/ERK kinases (MEKs), which are themselves activated by Ras/Raf proteins following cell stimulation. As such, these enzymes may present useful therapeutic targets. MAP kinases have several interesting properties, including a complex dual phosphorylation regulatory mechanism and a high substrate specificity for hydroxyamino acids that are followed by proline in the target protein's sequence. Few protein kinase systems have been thoroughly investigated and none has crystallographic data for both the inactive and active or phosphorylated forms of the same enzyme.