PROTEIN CRYSTAL STRUCTURE DETERMINATIONS RELATED TO NITRIC OXIDE SIGNALING

与一氧化氮信号传导相关的蛋白质晶体结构测定

• 批准号: 8362426
• 负责人: SUE L ROBERTS
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362426
• 关键词: Binding; Biological Models; Biology; Chemicals; Copper; Evolution; Funding; Grant; Heme; Homeostasis; Laboratories; Metal Binding Site; Metals; National Center for Research Resources; Nitric Oxide; Principal Investigator; Proteins; Radiation; Research; Research Infrastructure; Resolution; Resources; Rhodnius; S-Nitrosothiols; Signal Transduction; Site; Soluble Guanylate Cyclase; Source; Structure; Time; United States National Institutes of Health; cost; human TXN protein; nitrophorin; protein structure; structural biology; synchrotron radiation

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. We are requesting beam time to further on-¿going projects in the laboratories of four PIs. These projects include (1) Structural studies of proteins involved in nitric oxide signaling, with emphasis on soluble guanylate cyclase (sGC), its functional domains and its regulatory partners. Several sGC fragments have been expressed and small crystals obtained for two of these. Two model systems, nitrophorin 4(Rhodnius prolixus) and thioredoxin (human)are under study for understanding nitrosyl heme and S-¿nitrosocysteine chemical biology. Crystals of these proteins diffract past 1.¿.(2)Structures of proteins involved in copper transport and homeostasis(McEvoy);(3) Evolution of Cro and lipocalin proteins (Cordes), and (4) Structure/mechanism studies of QueD,(Bandarian)Crystals are available for all projects. Synchrotron radiation is needed for(1)MAD structure determination, (2) to provide sufficient resolution to determine accurate geometrical parameters such as heme distortion, metal binding site geometry and S-nitrosothiol geometry;(3) to provide variable wavelength x-¿rays for unambiguous identification of bound metal atoms and (4)to control photoreduction of metal sites and S-¿NO bonds.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 我们要求光束时间进一步进行四个PIS实验室的项目。这些项目包括（1）涉及一氧化氮信号传导的蛋白质的结构研究，重点是固体鸟苷酸环化酶（SGC），其功能域及其调节伙伴。已经表达了几个SGC片段，并为其中两个获得了小晶体。正在研究两个模型系统，分别是硝基磷酸蛋白4（Rhodnius prolixus）和硫氧还蛋白（人），以理解硝基糖基血红素和S-s-s-nitrosopysopysopsypspsateine Chemical Biology。这些蛋白质的晶体衍射过去是1.。（2）参与铜转运和稳态的蛋白质结构（MCEVOY）；（3）CRO和Lipocalin蛋白（Cordes）和（4）QUED的结构/机理研究（Bandarian）晶体的结构/机理研究的演变。 （1）MAD结构确定需要同步辐射，（2）提供足够的分辨率来确定准确的几何参数，例如血红素失真，金属结合位点几何和S-硝基硫醇几何形状；（3）为可变的波长X-€提供了可变的波长X-€射线，以使金属和（4）的金属粘合物均匀地识别金属和s-4）的金属位置。