CRYSTALLOGRAPHIC ANALYSIS OF MAP KINASES

描述：本研究项目的长期目标是了解 ERK 2的复杂调节机制，MAP激酶。 MAP激酶是 由激素启动的信号转导途径的重要元件， 细胞因子或环境压力。 MAP激酶如ERK 2被激活 在被MAP/ERK激酶（MEK）磷酸化后， 在细胞刺激后由Ras/Raf蛋白激活。 因此，这些 酶可以提供有用的治疗靶点。 MAP激酶有几个 有趣的性质，包括复杂的双重磷酸化调节 羟基氨基酸的高底物特异性， 接着是目标蛋白序列中的脯氨酸。 少量蛋白激酶 系统已被彻底调查，没有晶体学数据 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.