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首页> 美国卫生研究院文献>Biochemistry and Biophysics Reports >Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering
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Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering

机译：氘辅助小角中子散射表征免疫球蛋白G1 Fc糖蛋白与低亲和力Fcγ受体之间构象变形耦合相互作用

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A recently developed integrative approach combining varied types of experimental data has been successfully applied to three-dimensional modelling of larger biomacromolecular complexes. Deuteration-assisted small-angle neutron scattering (SANS) plays a unique role in this approach by making it possible to observe selected components in the complex. It enables integrative modelling of biomolecular complexes based on building-block structures typically provided by X-ray crystallography. In this integrative approach, it is important to be aware of the flexible properties of the individual building blocks. Here we examine the ability of SANS to detect a subtle conformational change of a multidomain protein using the Fc portion of human immunoglobulin G (IgG) interacting with a soluble form of the low-affinity Fcγ receptor IIIb (sFcγRIIIb) as a model system. The IgG-Fc glycoprotein was subjected to SANS in the absence and presence of 75%-deuterated sFcγRIIIb, which was matched out in D2O solution. This inverse contrast-matching technique enabled selective observation of SANS from IgG-Fc, thereby detecting its subtle structural deformation induced by the receptor binding. The SANS data were successfully interpreted by considering previously reported crystallographic data and an equilibrium between free and sFcγRIIIb-bound forms. Our SANS data thus demonstrate the applicability of SANS in the integrative approach dealing with biomacromolecular complexes composed of weakly associated building blocks with conformational plasticity.
机译：最近开发的结合各种类型的实验数据的集成方法已成功地应用于大型生物大分子复合物的三维建模。氘代辅助小角中子散射（SANS）在这种方法中起着独特的作用，因为它可以观察复合物中的选定成分。它可以基于通常由X射线晶体学提供的构件结构对生物分子复合物进行集成建模。在这种集成方法中，重要的是要意识到各个构建基块的灵活属性。在这里，我们使用人免疫球蛋白G（IgG）的Fc部分与低亲和力Fcγ受体IIIb（sFcγRIIIb）的可溶形式相互作用，研究了SANS检测多域蛋白微妙构象变化的能力。在不存在和存在75％氘代sFcγRIIIb的情况下，对IgG-Fc糖蛋白进行SANS处理，将其在D2O溶液中进行匹配。这种逆反比对技术可以从IgG-Fc中选择性观察SANS，从而检测其因受体结合而引起的细微结构变形。通过考虑先前报道的晶体学数据以及游离和sFcγRIIIb结合形式之间的平衡，成功解释了SANS数据。因此，我们的SANS数据证明了SANS在处理由具有构象可塑性的弱关联构建基组成的生物大分子复合物的综合方法中的适用性。

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