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。 摘要使用分子动力学（MD）模拟，计算蛋白修饰和热力学整合（TI）方法，我们将集中于研究Na/H交换调控因子1（NHERF1）的PDZ-配合配合物（NHERF1）的生物学和药用重要性。我们将研究PDZ2 - 配体相互作用。为了探测这种相互作用，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。