惊人的 HK97 折叠：微小差异带来多样结果。
The amazing HK97 fold: versatile results of modest differences.
机构信息
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States.
Departments of Molecular and Cell Biology, and Chemistry, University of Connecticut, Storrs, CT, 06269-3125, United States.
出版信息
Curr Opin Virol. 2019 Jun;36:9-16. doi: 10.1016/j.coviro.2019.02.001. Epub 2019 Mar 8.
Abstract
dsDNA Bacteriophages, some dsDNA archaeal viruses and the Herpesviruses share many features including a common capsid assembly pathway and coat protein fold. The coat proteins of these viruses, which have the HK97 fold, co-assemble with a free or attached scaffolding protein and other capsid proteins into a precursor capsid, known as a procapsid or prohead. The procapsid is a metastable state that increases in stability as a result of morphological changes that occur during the dsDNA packaging reaction. We review evidence from several systems indicating that proper contacts acquired in the assembly of the procapsid are critical to forming the correct morphology in the mature capsid.
摘要
dsDNA 噬菌体、一些 dsDNA 古菌病毒和疱疹病毒具有许多共同特征，包括共同的衣壳组装途径和衣壳蛋白折叠。这些病毒的衣壳蛋白具有 HK97 折叠，与游离或附着的支架蛋白以及其他衣壳蛋白一起组装成前体衣壳，称为原衣壳或原头。原衣壳是一种亚稳定状态，由于 dsDNA 包装反应过程中发生的形态变化，其稳定性增加。我们综述了来自几个系统的证据，表明在原衣壳组装过程中获得的适当接触对于在成熟衣壳中形成正确形态至关重要。
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