BINDING CAPACITY OF THE PDZ2 DOMAIN OF NHERF1

NHERF1 的 PDZ2 结构域的结合能力

• 批准号: 8364320
• 负责人: Peter A Friedman
• 金额: $ 0.11万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-15 至 2013-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364320
• 关键词: Affinity; Amino Acids; Binding; Biological; Biomedical Research; Complex; Funding; Grant; High Performance Computing; Ligands; Methods; National Center for Research Resources; Post-Translational Protein Processing; Principal Investigator; Research; Research Infrastructure; Resources; Source; Thermodynamics; United States National Institutes of Health; abstracting; cost; molecular dynamics

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. Abstract Using Molecular Dynamic (MD) simulations, computational protein modification, and Thermodynamic Integration (TI) method we will concentrate on the studying of the PDZ-ligand complexes of Na/H Exchange Regulatory Factor-1 (NHERF1) due to their biological and medicinal importance. We will investigate the PDZ2-ligand interactions. To probe such interactions we will use the five amino acid residue motifs WETVM (L1) or LFSNL (L2). We are planning to estimate binding affinity of PDZ2 for both L1 and L2.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 摘要：利用分子动力学 (MD) 模拟、计算蛋白质修饰和热力学积分 (TI) 方法，我们将集中研究 Na/H 交换调节因子 1 (NHERF1) 的 PDZ-配体复合物，因为它们具有生物学和药用价值。重要性。我们将研究 PDZ2-配体相互作用。为了探究这种相互作用，我们将使用五个氨基酸残基基序 WETVM (L1) 或 LFSNL (L2)。我们计划估计 PDZ2 对 L1 和 L2 的结合亲和力。