Tailed, double-stranded DNA bacteriophages provide a well-characterized model system for the study of viral assembly, especially for herpesviruses and adenoviruses. A wealth of genetic, structural, and biochemical work has allowed for the development of assembly models and an understanding of the DNA packaging process. The portal complex is an essential player in all aspects of bacteriophage and herpesvirus assembly. Despite having low sequence similarity, portal structures across bacteriophages share the portal fold and maintain a conserved function. Due to their dynamic role, portal proteins are surprisingly plastic, and their conformations change for each stage of assembly. Because the maturation process is dependent on the portal protein, researchers have been working to validate this protein as a potential antiviral drug target. Here we review recent work on the role of portal complexes in capsid assembly, including DNA packaging, as well as portal ring assembly and incorporation and analysis of portal structures.

中文翻译：

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门蛋白：双链 DNA 尾噬菌体和疱疹病毒衣壳组装的协调者。

有尾双链 DNA 噬菌体为病毒组装研究提供了一个特征良好的模型系统，尤其是疱疹病毒和腺病毒。大量的遗传、结构和生化工作使得装配模型的开发和对 DNA 包装过程的理解成为可能。门复合体在噬菌体和疱疹病毒组装的各个方面都是重要的参与者。尽管序列相似性较低，但噬菌体的门结构共享门折叠并保持保守的功能。由于其动态作用，门蛋白具有令人惊讶的可塑性，并且它们的构象在组装的每个阶段都会发生变化。由于成熟过程依赖于门户蛋白，研究人员一直致力于验证该蛋白作为潜在的抗病毒药物靶点。在这里，我们回顾了最近关于门静脉复合物在衣壳组装中的作用的工作，包括 DNA 包装，以及门静脉环组装以及门静脉结构的合并和分析。