School of Biosciences and Bioengineering, Indian Institute of Technology Mandi, Mandi, Himachal Pradesh, India.
Protein Sci. 2023 Nov;32(11):e4804. doi: 10.1002/pro.4804.
Any protein's flexibility or region makes it available to interact with many biomolecules in the cell. Specifically, such interactions in viruses help them to perform more functions despite having a smaller genome. Therefore, these flexible regions can be exciting and essential targets to be explored for their role in pathogenicity and therapeutic developments as they achieve essential interactions. In the continuation with our previous study on disordered analysis of SARS-CoV-2 spike protein's cytoplasmic tail (CTR), or endodomain, here we have explored the endodomain's disordered potential of six other coronaviruses using multiple bioinformatics approaches and molecular dynamics simulations. Based on the comprehensive analysis of its sequence and structural composition, we report the varying disorder propensity in endodomains of spike proteins of coronaviruses. The observations of this study may help to understand the importance of spike glycoprotein endodomain and creating therapeutic interventions against them.
任何蛋白质的灵活性或区域使其能够与细胞中的许多生物分子相互作用。具体来说,病毒中的这种相互作用有助于它们尽管基因组较小,但仍能执行更多功能。因此,这些灵活的区域可能是令人兴奋的和必要的目标,值得探索它们在致病性和治疗开发中的作用,因为它们实现了必要的相互作用。在前一项关于 SARS-CoV-2 刺突蛋白胞质尾(CTR)或内域无序分析的研究的基础上,在这里我们使用多种生物信息学方法和分子动力学模拟探索了另外六种冠状病毒的内域无序潜力。基于对其序列和结构组成的综合分析,我们报告了冠状病毒刺突蛋白内域的变异性无序倾向。这项研究的观察结果可能有助于理解刺突糖蛋白内域的重要性,并针对它们创造治疗干预措施。