Structural similarity of the binding sites of cyclophilin A-cyclosporin A and FKBP-FK506 systems.
Two enzymes, cyclophilin A and FK506-binding protein, with similar cis-trans isomerization catalytic activities but no similarity on the amino acid sequence level were compared in their three-dimensional structure by computer modelling. Cyclophilin A and FK506-binding protein proved to have similar arrangements at nine of the amino acids at their active site pockets. Two inhibitory peptides, cyclosporin A and FK506, also have structural similarities at their contact regions to the active sites. The studied systems may be another example of convergent evolution of enzyme catalytic site.
Denesyuk
A I
AI
Institute of Immunology, Moscow Region, Russia.
Vihinen
M
M
Lundell
J
J
Zav'yalov
V P
VP
Korpela
T
T
D000591:Amino Acid Isomerases / Q000737:chemistry*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D003198:Computer Simulation; D016572:Cyclosporine / Q000737:chemistry*; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D016559:Tacrolimus / Q000737:chemistry*; D022021:Tacrolimus Binding Proteins
D002352:Carrier Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus