Regulatory Mechanism for the reactive oxygen-producing enzyme family Nox

关于活性氧产生酶家族Nox（NADPH氧化酶）的作用机制，我们在本项目的过程中获得了以下结果。(1)我们发现，PX和PB 1结构域的p40 pax，参与Nox 2激活的蛋白质，调节易位的这种蛋白质的吞噬体膜之间的分子内相互作用，并确定了全长p40 phax的晶体结构。(2)我们确定了Nox 2区域，该区域参与Nox 2和Nox 2与p22 phax结合中的电子转移。(3)我们证明，Noxo 1，Nox 1的一个重要的激活剂，是保持在一个无活性的形式通过分子内相互作用，这是由翻译后修饰释放。(4)我们阐明了小的GTb-Rac通过与Noxa 1和p67 phax相互作用而作为Nox 1和Nox 3的激活剂发挥功能，分别(5)我们还表明，Rac 3能够作为Nox 1，Nox 2和Nox 3的调节因子，并且Rac 1 -3对Nox 1 -3的激活都不需要插入螺旋，这是一个对包括Rac在内的Rho家族GTP酶具有特异性的区域。

On the mechanism of the reactive oxygen-producing enzyme family Nox (NADPH oxidase), we obtained the following results during the course of this project. (1) We showed that an intramolecular interaction between the PX and PB1 domains of p40pax, a protein involved in Nox2 activation, regulates translocation of this protein to the phagosomal membrane, and also determined the crystal structure of the full-length p40phax. (2) We identified Nox2 regions, which participate in electron transfer in Nox2 and Nox2 binding to p22phax. (3) We demonstrated that Noxo1, an essential activator of Nox1, is kept in an inactive form via an intramolecular interaction, which is released by posttranslational modifications. (4) We clarified that the small GTPase Rac functions as an activator of Nox1 and Nox3 by interacting with Noxa1 and p67phax., respectively. (5) We also showed that Rac3 is capable of acting as a regulator of Nox1, Nox2, and Nox3, and that none of the activations of Nox1-3 by Rac1-3 requires the insert helix, a region specific to the Rho-family GTPases including Rac.