Cyclophilin A and an antibody against cyclosporin A resemble each other in their binding sites.
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.
Denesyuk
A I
AI
Institute of Immunology, Moscow Region, Russia.
Lundell
J
J
Zav'yalov
V
V
Korpela
T
T
D000591:Amino Acid Isomerases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D016572:Cyclosporine / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase; D011485:Protein Binding; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase