CRYSTAL STRUCTURES OF HUMAN POLYMERASE BETA COMPLEXED W/ DNA & NUCLEOTIDES

与 DNA 复合的人聚合酶 β 的晶体结构

• 批准号: 6119391
• 负责人: MARK A MILLER
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119391
• 关键词: biomaterials; proteins

We propose to use synchrotron radiation and the rotating camera on beam line 7-1 to collect a complete set of diffraction data on crystals of human DNA polymerase beta (pol _) complexed with DNA template-ddNTP mismatches. Pol _ is a eukaryotic DNA polymerase involved in the repair of damaged DNA. Specifically, pol &Beta has been shown to participate in the base excision repair (BER) pathway. Its small size (39 kD) makes pol &Beta a relativelly uncomplicated target for mechanistic studies of the nucleotidyl transfer reaction. High resolution data is needed to see the detail of conformational changes and how conformational changes promote fidelity.

我们建议使用同步加速器辐射和旋转相机 梁线7-1收集一组完整的衍射数据 与DNA复合的人DNA聚合酶β（pol _）的晶体 模板DDNTP不匹配。 POL _是真核DNA聚合酶 参与修复受损的DNA。 具体而言，Pol＆Beta具有 已显示参加基础切除修复（BER）途径。 它的尺寸很小（39 kd）使POL＆BETA成为相关的简单 核苷转移反应的机械研究靶标。 需要高分辨率数据来查看构象的细节 变化以及构象变化如何促进保真度。