Front Cover: Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering (ChemBioChem 22/2020),ChemBioChem

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Front Cover: Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering (ChemBioChem 22/2020)
ChemBioChem ( IF 2.6 ) Pub Date : 2020-10-28 , DOI: 10.1002/cbic.202000732
Alireza Ghanbarpour _{1,

2} , Elizabeth M. Santos _{1,

3} , Cody Pinger ₄ , Zahra Assar ₅ , Seyedmehdi Hossaini Nasr ₁ , Chrysoula Vasileiou ₁ , Dana Spence ₄ , Babak Borhan ₁ , James H. Geiger ₁

Affiliation

The folding pathway of human cellular retinol binding protein II was manipulated to favor formation of the shown domain‐swapped trimer, by rational protein engineering of a cross‐subunit disulfide bond. The inset shows the zinc binding site, engineered into the trimer with a single mutation, by exploiting the threefold axis of symmetry in the center of the trimer. The “purple flag” iris shows how the overall threefold symmetry positions the small, white inner petals, reflective of the three coordinating histidines in the trimer. More information can be found in the communication by J. H. Geiger et al.

中文翻译：

封面：人类细胞视黄醇结合蛋白II形成结构域交换的三聚体，代表蛋白质工程的新折叠和新模板（ChemBioChem 22/2020）

通过跨亚基二硫键的合理蛋白质工程，操纵了人类细胞视黄醇结合蛋白II的折叠途径，以利于形成所示的域交换三聚体。插图显示了通过利用三聚体中心的三重对称轴，将锌结合位点工程化为三聚体的单一突变。“紫色标记”虹膜显示整体三重对称如何定位白色的小内部花瓣，反映了三聚体中的三个配位组氨酸。在J. H. Geiger等人的来文中可以找到更多信息。

更新日期：2020-11-17

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