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首页> 外文期刊>Structure >Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure
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Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure

机译：具有混合α/β结构的异源四聚体21残基小蛋白的设计

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The study of short, autonomously folding peptides, or "miniproteins," is important for advancing our understanding of protein stability and folding specificity. Although many examples of synthetic a-helical structures are known, relatively few mixed alpha/beta structures have been successfully designed. Only one mixed-secondary structure oligomer, an alpha/beta homotetramer, has been reported thus far. In this report, we use structural analysis and computational design to convert this homotetramer into the smallest known alpha/beta-heterotetramer. Computational screening of many possible sequence/structure combinations led efficiently to the design of short, 21-residue peptides that fold cooperatively and autonomously into a specific complex in solution. A 1.95 Angstrom crystal structure reveals how steric complementarity and charge patterning encode heterospecificity. The first- and second-generation heterotetrameric miniproteins described here will be useful as simple models for the analysis of protein-protein interaction specificity and as structural platforms for the further elaboration of folding and function.
机译：短的，自主折叠的肽或“小蛋白”的研究对于增进我们对蛋白质稳定性和折叠特异性的理解很重要。尽管合成α-螺旋结构的许多实例是已知的，但已经成功设计了相对较少的混合α/β结构。迄今为止，仅报道了一种混合二级结构低聚物，即α/β同四聚体。在本报告中，我们使用结构分析和计算设计将该同四聚体转化为已知的最小的α/β-异四聚体。对许多可能的序列/结构组合的计算机筛选有效地导致了短的21位残基肽的设计，该肽可协同并自主折叠成溶液中的特定复合物。 1.95埃的晶体结构揭示了空间互补性和电荷构图如何编码异种特异性。本文所述的第一代和第二代异四聚体微蛋白将用作分析蛋白质-蛋白质相互作用特异性的简单模型，并用作进一步详细设计折叠和功能的结构平台。

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