PDF(Pubmed)
Abstract：
Antibodies are widely used in medicinal and scientific research due to their ability to bind to a specific antigen. Most often, antibodies are composed of heavy and light chain domains. Under physiological conditions, light chains are produced in excess, as compared to the heavy chain. It is now known that light chains are not silent partners of the heavy chain and can modulate the immune response independently. In this work, the first crystal structure of a light chain dimer originating from mice is described. It represents the light chain dimer of 6A8, a monoclonal antibody specific to the allergen Der f 1. Building on the unexpected occurrence of this kind of dimer, we have demonstrated that this light chain is stable in solution alone. Moreover, enzyme-linked immunosorbent assays (ELISA) have revealed that, when the light chain is not partnered to its corresponding heavy chain, it interacts non-specifically with a wide range of proteins. Computational studies were used to provide insight on the role of the 6A8 heavy chain domain in the specific binding to Der f 1. Overall, this work demonstrates and supports the ongoing notion that light chains can function by themselves and are not silent partners of heavy chains.
摘要：
抗体由于其与特定抗原结合的能力而广泛用于医学和科学研究。大多数情况下,抗体由重链和轻链结构域组成。在生理条件下,轻链是过量产生的，与重链相比。现在已知轻链不是重链的沉默伴侣,并且可以独立地调节免疫应答。在这项工作中,描述了源自小鼠的轻链二聚体的第一晶体结构。它代表6A8的轻链二聚体,一种特异于变应原Derf1的单克隆抗体。基于这种二聚体的意外发生，我们已经证明该轻链在单独的溶液中是稳定的。此外，酶联免疫吸附试验(ELISA)表明，当轻链未与其相应的重链配对时，它与多种蛋白质非特异性相互作用。计算研究用于提供对6A8重链结构域在与Derf1的特异性结合中的作用的见解。总的来说,这项工作证明并支持了正在进行的观点，即轻链可以自己发挥作用，而不是重链的沉默伴侣。
