Mariuzza R A, Poljak R J
Institut Pasteur, Paris, France.
Curr Opin Immunol. 1993 Feb;5(1):50-5. doi: 10.1016/0952-7915(93)90080-c.
New insights into the nature of antigen-antibody recognition have been gained through X-ray crystallographic studies of immune complexes. In particular, it has been demonstrated that water molecules form an extended network bridging antigen and antibody, and are essential in achieving shape and chemical complementarity between their interacting surfaces. This finding has important implications for the energetics of the association reaction. Recently, X-ray data on the complex between a peptide hormone and an anti-anti-idiotypic antibody have been obtained. This has relevance to the structural basis of antigen mimicry by antibodies. The conformation of the bound peptide was found to be very similar to that of an antibody complementarity determining region loop, providing a direct structural explanation for how antigen mimicry by anti-idiotypic antibodies might occur.
通过对免疫复合物的X射线晶体学研究,人们对抗抗原-抗体识别的本质有了新的认识。特别是,已经证明水分子形成了一个延伸的网络,连接抗原和抗体,并且对于实现它们相互作用表面之间的形状和化学互补性至关重要。这一发现对缔合反应的能量学具有重要意义。最近,已经获得了关于一种肽激素与一种抗抗独特型抗体之间复合物的X射线数据。这与抗体模拟抗原的结构基础相关。发现结合肽的构象与抗体互补决定区环的构象非常相似,为抗独特型抗体如何模拟抗原提供了直接的结构解释。