病毒的末端结合蛋白VPg(Viral Protein Genome-linked)是一种多功能蛋白,存在于多种病毒中,与病毒基因组RNA5′-末端共价连接,在病毒的生命周期中以不同的剪切形式存在并行使不同的功能,参与病毒的复制、翻译等基本的生命活动。主要对...病毒的末端结合蛋白VPg(Viral Protein Genome-linked)是一种多功能蛋白,存在于多种病毒中,与病毒基因组RNA5′-末端共价连接,在病毒的生命周期中以不同的剪切形式存在并行使不同的功能,参与病毒的复制、翻译等基本的生命活动。主要对目前关于VPg如何参与病毒的复制和翻译过程,以及在病毒蛋白质成熟和病毒移动过程中如何发挥作用的研究结果进行了综述。展开更多
Background:Computer simulation studies complement in vitro experiments and provide avenue to understand allosteric regulation in the absence of other molecular viewing techniques.Molecular dynamics captures internal m...Background:Computer simulation studies complement in vitro experiments and provide avenue to understand allosteric regulation in the absence of other molecular viewing techniques.Molecular dynamics captures internal motion within the protein and enables tracing the communication path between a catalytic site and a distal allosteric site.In this article,we have identified the communication pathway between the viral protein genome linked(VPg)binding region and catalytic active site in nuclear inclusion protein-a protease(NIa-Pro).Methods:Molecular dynamics followed by in silico analyses have been used to map the allosteric pathway.Results:This study delineates the residue interaction network involved in allosteric regulation of NIa-Pro activity by VPg.Simulation studies indicate that point mutations in the VPg interaction interface of NIa-Pro lead to disruption in these networks and change the orientation of catalytic residues.His142Ala and His167Ala mutations do not show a substantial change in the overall protease structure,but rather in the residue interaction network and catalytic site geometry.Conclusion:Our mutagenic study delineates the allosteric pathway and facilitates the understanding of the modulation of NIa-Pro activity on a molecular level in the absence of the structure of its complex with the known regulator VPg.Additionally,our in silico analysis explains the molecular concepts and highlights the dynamics behind the previously reported wet lab study findings.展开更多
文摘病毒的末端结合蛋白VPg(Viral Protein Genome-linked)是一种多功能蛋白,存在于多种病毒中,与病毒基因组RNA5′-末端共价连接,在病毒的生命周期中以不同的剪切形式存在并行使不同的功能,参与病毒的复制、翻译等基本的生命活动。主要对目前关于VPg如何参与病毒的复制和翻译过程,以及在病毒蛋白质成熟和病毒移动过程中如何发挥作用的研究结果进行了综述。
文摘Background:Computer simulation studies complement in vitro experiments and provide avenue to understand allosteric regulation in the absence of other molecular viewing techniques.Molecular dynamics captures internal motion within the protein and enables tracing the communication path between a catalytic site and a distal allosteric site.In this article,we have identified the communication pathway between the viral protein genome linked(VPg)binding region and catalytic active site in nuclear inclusion protein-a protease(NIa-Pro).Methods:Molecular dynamics followed by in silico analyses have been used to map the allosteric pathway.Results:This study delineates the residue interaction network involved in allosteric regulation of NIa-Pro activity by VPg.Simulation studies indicate that point mutations in the VPg interaction interface of NIa-Pro lead to disruption in these networks and change the orientation of catalytic residues.His142Ala and His167Ala mutations do not show a substantial change in the overall protease structure,but rather in the residue interaction network and catalytic site geometry.Conclusion:Our mutagenic study delineates the allosteric pathway and facilitates the understanding of the modulation of NIa-Pro activity on a molecular level in the absence of the structure of its complex with the known regulator VPg.Additionally,our in silico analysis explains the molecular concepts and highlights the dynamics behind the previously reported wet lab study findings.
