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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Structure of a hydrophobic leucinostatin derivative determined by host lattice display
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Structure of a hydrophobic leucinostatin derivative determined by host lattice display

机译：Structure of a hydrophobic leucinostatin derivative determined by host lattice display

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摘要

Peptides comprising many hydrophobic amino acids are almost insoluble under physiological buffer conditions, which complicates their structural analysis. To investigate the three-dimensional structure of the hydrophobic leucinostatin derivative ZHAWOC6027, the previously developed host lattice display technology was applied. Two designed ankyrin-repeat proteins (DARPins) recognizing a biotinylated ZHAWOC6027 derivative were selected from a diverse library by ribosome display under aqueous buffer conditions. ZHAWOC6027 was immobilized by means of the DARPin in the host lattice and the structure of the complex was determined by X-ray diffraction. ZHAWOC6027 adopts a distorted alpha-helical conformation. Comparison with the structures of related compounds that have been determined in organic solvents reveals elevated flexibility of the termini, which might be functionally important.
机译：肽组成许多疏水性氨基酸几乎不溶性在生理缓冲条件,复杂的结构分析。疏水leucinostatin的结构导数ZHAWOC6027,之前开发的主点阵显示技术应用。设计ankyrin-repeat蛋白(DARPins)认识到生物素化的ZHAWOC6027导数选择从不同的图书馆通过核糖体水缓冲条件下显示。ZHAWOC6027通过DARPin目瞪口呆在主晶格的结构复杂的是由x射线衍射。ZHAWOC6027采用一种扭曲的α螺旋构象。相关的化合物已被确定有机溶剂揭示了高架的灵活性目的地,可能的功能重要的。

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