Leroux Makayla N, Skidds Garrett S, Teschke Carolyn M
Department of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Rd, Storrs, CT, 06269-3125, USA.
Department of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Rd, Storrs, CT, 06269-3125, USA; Department of Chemistry, University of Connecticut, 55 N. Eagleville Rd, Storrs, CT, 06269-3060, USA.
Curr Opin Struct Biol. 2025 Jun 16;94:103081. doi: 10.1016/j.sbi.2025.103081.
Icosahedral double stranded DNA (dsDNA) virus assembly first necessitates the formation of a precursor capsid (procapsid) into which the DNA is packaged. Direct interactions between the major capsid protein (MCP) and a scaffolding protein promote proper procapsid assembly. The scaffolding protein can be an independent protein or a scaffolding-like domain covalently attached to the MCP that is comparable in structure and function. A full understanding of scaffolding protein structures has been limited by their intrinsically disordered nature. Advances in cryogenic electron microscopy (cryoEM) data processing techniques have provided new methodologies to help solve the structures of scaffolding proteins within procapsids. These structural insights further our understanding of how scaffolding proteins interact with the other assembly proteins to correctly construct the procapsid.
二十面体双链DNA（dsDNA）病毒组装首先需要形成一个前体衣壳（原衣壳），DNA被包装到其中。主要衣壳蛋白（MCP）与支架蛋白之间的直接相互作用促进了原衣壳的正确组装。支架蛋白可以是一种独立的蛋白质，也可以是一个与MCP共价连接的支架样结构域，其结构和功能具有可比性。对支架蛋白结构的全面理解一直受到其内在无序性质的限制。低温电子显微镜（cryoEM）数据处理技术的进步提供了新的方法，有助于解析原衣壳内支架蛋白的结构。这些结构上的见解进一步加深了我们对支架蛋白如何与其他组装蛋白相互作用以正确构建原衣壳的理解。
