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Assessment of the robustness of a serendipitous zinc binding fold: Mutagenesis and protein grafting

机译：评估意外的锌结合折叠的稳健性：诱变和蛋白质嫁接

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摘要

Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates.
机译：锌结合基序在蛋白质设计领域受到了广泛关注。在这里，我们测试了最近发现的非天然锌结合结构作为蛋白质设计支架的适用性。创建了一系列多个丙氨酸突变体以研究折叠的最低要求，并且这些突变体的溶液结构显示，尽管序列的50％发生了变化，但仍保持了原始折叠。接下来，我们尝试将结合的面孔从选定的双分子相互作用移植到这些突变体中的一个上，并且显示许多产生的“嵌合体”采用了天然样的折叠。这些结果既突出了小锌结合结构域的鲁棒性，又强调了设计功能蛋白的复杂性，即使使用这种小而高度有序的支架作为模板也是如此。

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