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首页> 外文期刊>Biochemistry >NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB
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NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB

机译：钩端螺旋体宿主相互作用的外部膜蛋白LigB的末端免疫球蛋白样域的NMR解决方案结构。

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摘要

A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown promise as a marker in typing leptospiral isolates for pathogenesis and as an antigen in vaccines. We used NMR spectroscopy to solve the solution structure of the twelfth immunoglobulin-like (Ig-like) repeat domain from LigB (LigB-12). The fold is similar to that of other bacterial Ig-like domains and comprised mainly of β-strands that form a β-sandwich based on a Greek-key folding arrangement. Based on sequence analysis and conservation of structurally important residues, homology models for the other LigB Ig-like domains were generated. The set of LigB models illustrates the electrostatic differences between the domains as well as the possible interactions between neighboring domains. Understanding the structure of the extracellular portion of LigB and related proteins is important for developing diagnostic methods and new therapeutics directed toward leptospirosis.
机译：已经鉴定出许多对钩端螺旋体致病菌株具有特异性的表面蛋白。 Lig蛋白家族已显示出有望作为键入钩端螺旋体分离株的标志物用于发病机理，并有望作为疫苗中的抗原。我们使用NMR光谱法解决了LigB（LigB-12）中第十二个免疫球蛋白样（Ig样）重复域的溶液结构。折叠类似于其他细菌Ig样结构域的折叠，并且主要由基于希腊-关键折叠排列形成β-三明治的β-链组成。基于序列分析和结构上重要的残基的保守性，生成其他LigB Ig样域的同源性模型。 LigB模型集说明了域之间的静电差异以及相邻域之间的可能相互作用。了解LigB和相关蛋白的胞外部分的结构对于开发针对钩端螺旋体病的诊断方法和新疗法非常重要。

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