STRUCTURE BASED APPROACH TO ISSUES IN ZINC FINGER RECOGNITION

基于结构的方法解决锌指识别问题

• 批准号: 7370576
• 负责人: Nancy C Horton
• 金额: $ 0.3万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370576
• 关键词: STRUCTURE; BASED; APPROACH; ISSUES; ZINC

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Aart is a six-finger zinc finger protein designed by Prof. David Segal in the Barbas lab at the Scripps Research Institute. It is an excellent choice for crystallographic studies because several of the nucleotide triads it binds are unusual and because it may offer insight into the strain associated with zinc finger proteins longer than three fingers in length. The protein has been crystallized in this lab previously. A complete native data set has been collected to 2.95 ¿¿at APS BL 14-BMC (P1 a = 40.57 ¿¿b = 69.09 ¿¿c = 70.84 ¿¿alpha = 101.18¿¿ beta = 94.36¿¿ gamma = 105.30¿¿) there are two protein molecules and two twenty-two base pair DNA duplexes in the asymmetric unit. Synchrotron radiation is necessary for high resolution data collection as well as structure solution. Multi wavelength anomalous dispersion data collection is planned using brominated DNA derivatives of this crystal form.

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。AART是斯克里普斯研究所Barbas实验室的大卫·西格尔教授设计的一种六指锌指蛋白。它是结晶学研究的绝佳选择，因为它结合的几个核苷酸三联体是不寻常的，而且它可能提供与锌指蛋白相关的菌株的洞察，长度超过三个手指。这种蛋白质以前曾在这个实验室中结晶过。在APS BL14-BMC(P1a=40.57b=69.09c=70.84α=101.18β=94.36伽马=105.30)有两个蛋白质分子和两个22个碱基对的DNA二聚体。同步辐射是高分辨率数据采集和结构解算所必需的。计划使用这种晶体形式的溴化DNA衍生物收集多波长异常色散数据。