STRUCTURAL DETERMINATION OF N TERMINAL SH2 DOMAIN FR GTPASE ACTIVATING

GTP结合蛋白ras是细胞增殖的关键蛋白 信号通路 ras的突变形式已经在许多人中发现， 动物和人类肿瘤细胞。 最重要的负面影响之一 调节蛋白是GTP酶激活蛋白（GAP），其催化 Ras蛋白中GTP水解为GDP，从而使Ras保持在其 不活跃的国内生产总值约束国。 GAP的N-末端SH 2结构域是 对于其与ras激活受体的结合至关重要，并且具有 在衍生自以下的五肽的存在下结晶 血小板衍生生长因子受体（PDGFR）。 晶体 在理学旋转阳极X射线源上衍射到3.0 E， RAXISII图像板。 初步实验表明，使用 同步辐射将提高数据的质量和分辨率 收集。

The GTP binding protein ras is a key protein in cell proliferation signaling pathways. Mutated forms of ras have been found in many animal and human tumor cells. One of the most important negative regulatory protein is GTPase activating protein (GAP), that catalyzes the hydrolysis of GTP in ras protein to GDP, thus keeping ras in its inactive GDP bound state. The N-terminal SH2 domain of GAP is essential for its association with ras activating receptors, and has been crystallized in the presence of a pentapeptide derived from platelet derived growth factor receptor (PDGFR). The crystals diffracted to 3.0 E on a Rigaku rotating anode X-ray source with RAXISII image plates. Preliminary experiments show that the use of synchrotron radiation will improve the quality and resolution of data collected.