GEOFF CHANG PRT-CRYSTALLOGRAPHY OF INTEGRAL MEMBRANE PROTEINS

Geoff Chang PRT-完整膜蛋白的晶体学

• 批准号: 7721800
• 负责人: GEOFFREY A CHANG
• 金额: $ 0.15万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721800
• 关键词: Cell Membrane Permeability; Cells; Class; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Data; Excision; Family; Funding; Goals; Grant; Health; Institution; Integral Membrane Protein; Lipid Bilayers; Medical; Membrane Proteins; Multi-Drug Resistance; Pharmaceutical Preparations; Phenotype; Rate; Research; Research Personnel; Resources; Series; Source; Structure; United States National Institutes of Health; base; efflux pump

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. Multi-drug resistance is a very significant health problem that has both medical and pharmacological concerns. The cause of the mdr phenotype is the result of a net decrease in the concentration of drug levels within the cell. This reduction occurs by two fundamental mechanisms that either lowers the membrane permeability, which leads to a decreased rate of drug entry across the lipid bilayer (Class I), or directly increasing the rate of drug removal from the cell (Class II). Both of these mechanisms are accomplished via a series of energy-dependent energy efflux pumps. Recently, we have obtained 3D crystals of a second distinct class of mdr transporters (Class II). The goal of this proposal is to determine the atomic structure of these mdr transporters. Hence, we will be able to discover the structural basis of mdr for this family of integral membrane proteins. We propose to screen and collect data from our membrane protein crystals and solve the structure of mdr transporter at SSRL.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 多药耐药性是一个非常重大的健康问题，既有医学和药理问题。 MDR表型的原因是细胞内药物水平浓度的净降低的结果。这种降低是通过两种基本机制进行的，这些机制要么降低膜渗透性，从而导致降低脂质双层（I类）的药物进入率降低，或者直接增加了从细胞中去除药物的速率（II类）。这两种机制都是通过一系列能量依赖的能量外泵来完成的。最近，我们获得了第二个不同类别转运蛋白类别的3D晶体（II类）。该提案的目的是确定这些MDR转运蛋白的原子结构。因此，我们将能够发现该整体膜蛋白家族的MDR的结构基础。我们建议从我们的膜蛋白晶体中筛选和收集数据，并在SSRL处解决MDR转运蛋白的结构。