Rouvinen J, Rautiainen J, Virtanen T, Zeiler T, Kauppinen J, Taivainen A, Mäntyjärvi R
Department of Chemistry, University of Joensuu, POB 111, FIN-80101 Joensuu, Finland.
J Biol Chem. 1999 Jan 22;274(4):2337-43. doi: 10.1074/jbc.274.4.2337.
The three-dimensional structure of the major bovine allergen Bos d 2 has been determined by using x-ray diffraction at 1.8-A resolution. Structurally Bos d 2 is a member of the lipocalin family comprising proteins with transport functions. There is a flat small cavity inside the Bos d 2 protein core suitable for ligand binding, and it is possible that Glu115 and Asn37 inside the core are able to make hydrogen bonds with the ligand. Many allergens from different animals belong to the lipocalin family. The amino acid residue similarities between these lipocalins indicate putative regions for IgE binding. Comparison with the available allergen structures from other sources suggests that these allergens are roughly the same size and that their shape is more spherical than elliptical.
通过1.8埃分辨率的X射线衍射确定了主要牛过敏原Bos d 2的三维结构。从结构上看,Bos d 2是脂质运载蛋白家族的成员,该家族蛋白具有运输功能。Bos d 2蛋白核心内部有一个扁平的小腔,适合配体结合,并且核心内部的Glu115和Asn37有可能与配体形成氢键。许多来自不同动物的过敏原都属于脂质运载蛋白家族。这些脂质运载蛋白之间的氨基酸残基相似性表明了IgE结合的推定区域。与其他来源的可用过敏原结构进行比较表明,这些过敏原大小大致相同,并且它们的形状更接近球形而非椭圆形。