MOLECULAR DYNAMICS SIMULATIONS OF THE ACTIVATION OF THE ADENOVIRUS PROTEINASE B

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 本项目的目的是通过分子动力学模拟来确定腺病毒蛋白水解酶(AVP)被其11个氨基酸的肽辅因子(PVIc)激活的结构基础。失活酶(AVP)和激活酶(AVP-pVIc)的晶体结构是已知的。对这些结构的分析表明，当pVIc与AVP结合时，激活可能通过一系列连续的结构变化的信号转导途径发生。分子动力学模拟将被用来确定结构变化的顺序。未来，分子动力学模拟的结果将用于基于结构的药物设计，以获得抗病毒药物。

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. The objective of this project is to determine the structural basis for the activation of the adenovirus proteinase (AVP) by its 11-amino-acid peptide cofactor (pVIc) using molecular dynamics simulations. Crystal structures of the inactive enzyme (AVP) and of the activated enzyme (AVP-pVIc) are known. Analysis of these structures indicates that upon the binding of pVIc to AVP activation may occur via a signal transduction pathway involving a series of contiguous structural changes. Molecular dynamics simulations will be used to determine the sequence of structural changes. In the future, the results of the molecular dynamics simulations will be used with structure-based drug design to obtain anti-viral agents.