STRUCTURAL DETERMINATION OF N TERMINAL SH2 DOMAIN FR GTPASE ACTIVATING

N 端 SH2 结构域 FR GTP 酶激活的结构测定

• 批准号: 6658493
• 负责人: SUNG-HOU KIM
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6658493
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; neoplasm /cancer; proteins; radiography; structural biology

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.

GTP结合蛋白ras是细胞增殖的关键蛋白。 信号通路。在许多疾病中发现了突变形式的ras 动物和人类的肿瘤细胞。最重要的负面影响之一 调节蛋白是GTP酶激活蛋白(GAP)，催化 Ras蛋白中GTP的水解为gdp，从而使ras保持在其 非活动GDP绑定状态。GAP N端SH2结构域是 对于它与ras激活受体的联系是必不可少的，并具有 在五肽存在下结晶 血小板衍生生长因子受体(PDGFR)。水晶 在Rigaku旋转阳极X射线源上衍射到3.0E RAXISII图像板。初步实验表明，该方法具有较高的实用价值 同步辐射将提高数据的质量和分辨率 收好了。