Denesyuk A I, Lundell J, Zav'yalov V, Korpela T
Institute of Immunology, Moscow Region, Russia.
Immunol Lett. 1994 Jul;41(2-3):213-6. doi: 10.1016/0165-2478(94)90135-x.
The three-dimensional structures of cyclosporin A complexed with cyclophilin A or Fab fragment of a monoclonal antibody were compared. In these two complexes conformations of the fragment D-alanine8-N-methylvaline11 in cyclosporin A were in a good agreement. In addition, cyclophilin A and the Fab fragment had related arrangements of the aromatic amino acids in their binding sites, implying that antibody independently utilizes similar structural themes for binding cyclosporin A as cyclophilin A.
比较了环孢菌素A与亲环蛋白A或单克隆抗体Fab片段复合后的三维结构。在这两种复合物中，环孢菌素A中D-丙氨酸8-N-甲基缬氨酸11片段的构象高度一致。此外，亲环蛋白A和Fab片段在其结合位点具有相关的芳香族氨基酸排列，这意味着抗体独立地利用与亲环蛋白A类似的结构模式来结合环孢菌素A。
