STRUCTURE OF CDC42HS IN COMPLEX W/ CATALYTIC DOMAIN OF CDC42GAP

具有 CDC42GAP 催化域的复杂 CDC42HS 结构

• 批准号: 6667813
• 负责人: Nicolas Nassar
• 金额: $ 14.27万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-09-30 至 2003-08-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6667813
• 关键词: bioimaging /biomedical imaging; biological products; biomedical resource; proteins; radiography; structural biology

Our first experiment was the structure determination of a cytoplasmic domain from a voltage-gated potassium channel. The domain contains 140 amino acids and controls the gating of a potassium channel that is responsible for electrical conduction in the heart. Synchrotron radiation was required because of the microscopic size of the crystals (50 microns) and because of severe nonisomorphism upon heavy atom derivitization. Protein containing selenomethionine was produced and the structure was solved in a 3 wavelength MAD experiment at F2 with data to 2.6
. The structure directly led to a hypothesis for the mechanism by which the domain regulates gating of the channel. The hypothesis has been tested through functional studies over the eight months since the structure determination and a paper is being written. Our second experiment was the structure determination of an integral membrane potassium channel using the A1 facility. The structure was solved by MIR with data to 3.2
and required numerous data collection sessions for both native and derivative sets. This structure forms the basis for our current understanding of potassium selectivity in ion channels. 4.

我们的第一个实验是确定 来自电压门控钾通道的细胞质结构域。 域名 含有 140 个氨基酸并控制钾的门控 负责心脏电传导的通道。 由于其微观尺寸，需要同步加速器辐射 晶体（50微米）并且由于严重的非同构性 重原子衍生化。 含有硒代蛋氨酸的蛋白质 产生并在 3 波长 MAD 实验中解析结构 在 F2 处，数据为 2.6 。该结构直接引出了一个假设 用于域调节通道门控的机制。 该假设已通过功能研究得到检验 自结构确定和论文正在撰写以来已有八个月了 书面。 我们的第二个实验是结构测定 使用 A1 设施的积分膜钾通道。 这 结构由 MIR 求解，数据为 3.2，需要大量 本机集和衍生集的数据收集会话。 这 结构构成了我们目前对钾的理解的基础 离子通道的选择性。 4.