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Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers

机译：氟离子通道和合成蛋白质阻滞剂之间的分子相互作用

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摘要

Fluoride ion channels of the Fluc family selectively export F~(–) ions to rescue unicellular organisms from acute F~(–) toxicity. Crystal structures of bacterial Fluc channels in complex with synthetic monobodies, fibronectin-derived soluble β-sandwich fold proteins, show 2-fold symmetric homodimers with an antiparallel transmembrane topology. Monobodies also block Fluc F~(–) current via a pore blocking mechanism. However, little is known about the energetic contributions of individual monobody residues to the affinity of the monobody–channel complex or whether the structural paratope corresponds to functional reality. This study seeks to structurally identify and compare residues interacting with Fluc between two highly similar monobodies and subjects them to mutagenesis and functional measurements of equilibrium affinities via a fluorescence anisotropy binding assay to determine their energetic contributions. The results indicate that the functional and structural paratopes strongly agree and that many Tyr residues at the interface, while playing a key role in affinity, can be substituted with Phe and Trp without large disruptions.
机译：氟化物家族的氟离子通道选择性地出口F〜（ - - ）离子以拯救急性F〜（ - ）毒性的单细胞生物。细菌琥珀色通道的晶体结构与合成单极性的络合物，纤连蛋白衍生的可溶性β-夹层折叠蛋白，显示出2倍对称同源体的反平行跨膜拓扑。 Monobodies还通过孔阻挡机构阻止熔丝F〜（ - ）电流。然而，关于单体型沟道复合物的亲和力或结构解析率对应于功能现实的少量对单一单体残留物的能量贡献几乎熟知。该研究旨在在结构上识别和比较与两个高度相似的单一的膀胱相互作用的残留物，并通过荧光各向异性结合测定来诱变和功能测量平衡亲态的均衡，以确定它们的能量贡献。结果表明，功能性和结构令人统治强烈同意并且在界面处的许多Tyr残留物，同时在亲和力中发挥关键作用，可以用PHE和TRP代替没有大的破坏。

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  • 来源
    《Biochemistry》 |2018年第7期|共7页
  • 作者

    Daniel L. Turman; Abraham Z. Cheloff; Alexis D. Corrado; Jacob T. Nathanson; Christopher Miller;

  • 作者单位

    Department of Biochemistry Howard Hughes Medical Institute Brandeis University 415 South Street Waltham Massachusetts 02453 United States;

    Department of Biochemistry Howard Hughes Medical Institute Brandeis University 415 South Street Waltham Massachusetts 02453 United States;

    Department of Biochemistry Howard Hughes Medical Institute Brandeis University 415 South Street Waltham Massachusetts 02453 United States;

    Department of Biochemistry Howard Hughes Medical Institute Brandeis University 415 South Street Waltham Massachusetts 02453 United States;

    Department of Biochemistry Howard Hughes Medical Institute Brandeis University 415 South Street Waltham Massachusetts 02453 United States;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
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