STRUCTURAL STUDIES OF PROTEINS INVOLVED IN APOPTOSIS

在SSRL的光束线9-1或7-1上请求时间， 三种不同蛋白质系统的分辨率结构测定。 一个系统涉及抑制细胞凋亡的病毒蛋白， 生物体去除多余细胞的过程。 凋亡是 对正常的有机体发育和组织平衡至关重要。 目前，一种蛋白质p35已经被克隆、结晶，其 已经使用来自旋转的X射线能量确定了结构， 阳极 此外，我的实验室正在积极研究 病毒蛋白质和蛋白质之间的复合物的结晶 它结合并抑制的细胞酶。 第二系统 包括蛋白质，它吸收来自 环境转化为生物体。 目前，水晶已经 获得的APS激酶，催化硫的第二步， activation. 我们也在积极追求 酶，ATP硫酸化酶，它催化第一个承诺的步骤。 最后一个请求时间的系统是在一个类似泛素的 蛋白质（RUB 1）参与细胞周期调控。 这 使用仅105米厚的晶体测定了小的蛋白质结构 用内部X射线，分辨率可达1.7 E。 高 来自SSRL的通量肯定会产生更高质量的数据， 所有三种蛋白质结构的分辨率更高。

Time is requested on beam line 9-1 or 7-1 at SSRL for high resolution structure determination of three different protein systems. One system involves viral proteins that inhibit apoptosis, an active process by which organisms remove superfluous cells. Apoptosis is vital to normal organismal development and tissue homeostasis. Currently one protein, p35, has been cloned, crystallized, and its structure has been determined using x-ray energy from a rotating anode. Additionally, my laboratory is actively pursuing crystallization of complexes between the viral protein and the cellular enzyme in which it binds and inhibits. The second system involves proteins that assimilate inorganic sulfur from the environment into living organisms. Currently crystals have been obtained of APS kinase, which catalyzes the second step in sulfur activation. We are also vigorously pursuing crystallization of the enzyme, ATP sulfurylase, which cayalyzes the first committed step. The last system for which time is requested in on a ubiquitin-like protein (RUB1) that is implicated in cell cycle regulation. This small protein structure was determined using crystals only 105m thick with in-house x-rays, which diffract to 1.7 E resolution. The high flux from SSRL will surely result in higher quality data at much higher resolution for all three protein structures.