A1 DOMAIN OF VON WILLEBRAND FACTOR COMPLEXES; AND BACTERIAL SIGNAL TRANSDUCTION

冯·威勒布兰德因子复合物的 A1 域；

• 批准号: 7721736
• 负责人: KOTTAYIL I VARUGHESE
• 金额: $ 0.06万
• 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/7721736
• 关键词: Affinity; Anthrax disease; Bacillus anthracis; Binding; Blood Platelets; Complex; Computer Retrieval of Information on Scientific Projects Database; Crystallization; DNA; Data; Disease; Extracellular Matrix; Funding; Glycoproteins; Grant; Growth; Hemorrhage; Institution; Membrane; Modeling; Myocardial Infarction; Platelet Membrane Glycoproteins; Process; Proteins; Rate; Research; Research Personnel; Resources; Signal Transduction; Site; Snake Venoms; Source; Structure; Thrombus; United States National Institutes of Health; botrocetin; promoter; receptor; transcription factor; von Willebrand Factor; wound

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. Binding of the platelet membrane glycoprotein (GP) Ibalpha to von Willebrand Factor (vWF) immobilized on the vessel wall initiates thrombus formation. This process, essential to arrest bleeding at wound sites, may also contribute to thrombotic diseases such as myocardial infarction, and is modulated by the affinity of vWF for platelets. At wall shear rates of 1500 s^(-1) or greater, platelet tethering to extracellular matrix components and thrombus growth depend on GP Ibalpha binding to the vWF A1 domain. We have determined the crystal structures the A1 domain of vWF and a modulator of A1 domain function- a snake venom protein, botrocetin. Now we have collected Pt MAD data on the platelet membrane receptor GP Ibalpha and the model building is in progress. We are in the process of crystallizing complexes of the GP Ibalpha with the A1 domain and the modulator botrocetin. 2. Bacterial phosphorelay proteins are investigated. Recently we solved the structure of the transcription factor Spo0A from B. subtilis in complex with a DNA duplex containing the recognition sequence. Crystallization of the transcription factor in complex with other promotor sequences are in progress. Spo0A initiates sporulation. Anthrax is caused by B. anthracis and its transcription factor is almost identical with that of B. subtilis.

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。 血小板膜糖蛋白（GP）Ibalpha与固定在血管壁上的von Willebrand因子（VWF）的结合启动了血栓形成。 在伤口部位阻止出血的必不可少的过程也可能导致血栓性疾病，例如心肌梗塞，并且受VWF对血小板的亲和力的调节。 以1500 s^（-1）或更大的壁剪切速率，血小板将细胞外基质组件的束缚和血栓生长取决于与VWF A1结构域结合的GP ibalpha。 我们已经确定了VWF的A1结构域和A1结构域功能的调节剂的晶体结构 - 蛇毒蛋白Botrocetin。 现在，我们已经收集了血小板膜受体GP Ibalpha的PT MAD数据，并且正在进行模型构建。我们正在与A1结构域和调节蛋白的GP Ibalpha的复合物结晶过程中。 2。研究细菌磷酸蛋白。 最近，我们与含有识别序列的DNA双链体中的复合物中的转录因子SPO0A的结构解决了。 与其他启动子序列复合物中转录因子的结晶正在进行中。 SPO0A启动孢子形成。 炭疽是由炭疽芽孢杆菌引起的，其转录因子几乎与枯草芽孢杆菌相同。