Gronenborn A M, Clore G M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20814.
J Mol Biol. 1993 Oct 5;233(3):331-5. doi: 10.1006/jmbi.1993.1514.
The B1 domain of streptococcal protein G interacts with the C-terminal fragment of the heavy chain of immunoglobulin G (IgGFc). The binding site for the protein G domain on the antibody fragment is in close proximity or overlapping with that determined for staphylococcal protein A. The interaction of the B1 domain with IgGFc was investigated by 1H-15N correlation spectroscopy. The major interaction site on the B1 domain comprises parts of beta-strand 3 as well as the alpha-helix. Comparison with the crystal structure of the protein A/IgGFc complex suggests that the mode of interaction in the two complexes is analogous, despite the lack of sequence or structural similarity between two antibody binding proteins.
链球菌蛋白G的B1结构域与免疫球蛋白G（IgG Fc）重链的C末端片段相互作用。蛋白G结构域在抗体片段上的结合位点与葡萄球菌蛋白A的结合位点紧密相邻或重叠。通过1H-15N相关光谱研究了B1结构域与IgG Fc的相互作用。B1结构域上的主要相互作用位点包括β链3的部分以及α螺旋。与蛋白A/I IgG Fc复合物的晶体结构比较表明，尽管两种抗体结合蛋白之间缺乏序列或结构相似性，但两种复合物中的相互作用模式是相似的。
