title: Structural similarity of the binding sites of cyclophilin A-cyclosporin A and FKBP-FK506 systems.
abstract: 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.
authors.affiliation: Institute of Immunology, Moscow Region, Russia.
authors.forename: A I
authors.initials: AI
authors.lastname: Denesyuk
authors.forename: M
authors.initials: M
authors.lastname: Vihinen
authors.forename: J
authors.initials: J
authors.lastname: Lundell
authors.forename: V P
authors.initials: VP
authors.lastname: Zav'yalov
authors.forename: T
authors.initials: T
authors.lastname: Korpela
mesh_terms: 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
chemical_list: D002352:Carrier Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus