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Solution structure, copper binding and backbone dynamics of recombinant Ber e 1 : the major allergen from brazil nut

机译:重组Bere 1的溶液结构,铜结合和骨架动力学:巴西坚果的主要过敏原

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摘要

BACKGROUND: The 2S albumin Ber e 1 is the major allergen in Brazil nuts. Previous findings indicated that the protein alone does not cause an allergenic response in mice, but the addition of components from a Brazil nut lipid fraction were required. Structural details of Ber e 1 may contribute to the understanding of the allergenic properties of the protein and its potential interaction partners. METHODOLOGY/PRINCIPAL FINDINGS: The solution structure of recombinant Ber e 1 was solved using NMR spectroscopy and measurements of the protein back bone dynamics at a residue-specific level were extracted using (15)N-spin relaxation. A hydrophobic cavity was identified in the structure of Ber e 1. Using the paramagnetic relaxation enhancement property of Cu(2+) in conjunction with NMR, it was shown that Ber e 1 is able to specifically interact with the divalent copper ion and the binding site was modeled into the structure. The IgE binding region as well as the copper binding site show increased dynamics on both fast ps-ns timescale as well as slower µs-ms timescale. CONCLUSIONS/SIGNIFICANCE: The overall fold of Ber e 1 is similar to other 2S albumins, but the hydrophobic cavity resembles that of a homologous non-specific lipid transfer protein. Ber e 1 is the first 2S albumin shown to interact with Cu(2+) ions. This Cu(2+) binding has minimal effect on the electrostatic potential on the surface of the protein, but the charge distribution within the hydrophobic cavity is significantly altered. As the hydrophobic cavity is likely to be involved in a putative lipid interaction the Cu(2+) can in turn affect the interaction that is essential to provoke an allergenic response.
机译:背景:2S白蛋白Ber e 1是巴西坚果中的主要过敏原。先前的发现表明,单独的蛋白质不会在小鼠中引起过敏反应,但是需要添加巴西坚果脂质组分中的成分。 Ber e 1的结构细节可能有助于理解蛋白质及其潜在相互作用伴侣的变应原性质。方法/主要发现:重组Bere 1的溶液结构使用NMR光谱解析,并使用(15)N-spin弛豫提取了特定残基水平的蛋白质背骨动力学。在Ber e 1的结构中鉴定出疏水腔。利用Cu(2+)的顺磁性弛豫增强特性与NMR结合,表明Ber e 1能够与二价铜离子发生特异性相互作用并形成结合网站已建模为结构。 IgE结合区以及铜结合位点在快速ps-ns时标和较慢的µs-ms时标上均显示出增加的动态。结论/意义:Ber e 1的总体折叠与其他2S白蛋白相似,但疏水腔类似于同源的非特异性脂质转移蛋白。 Ber e 1是第一个2S白蛋白,显示与Cu(2+)离子相互作用。这种Cu(2+)结合对蛋白质表面的静电势具有最小的影响,但疏水腔内的电荷分布却发生了显着变化。由于疏水腔可能与推定的脂质相互作用有关,因此Cu(2+)可能进而影响相互作用,而该相互作用对于引起过敏反应至关重要。

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