title: Molecular modeling studies in the complex between cyclophilin and cyclosporin A.
abstract: The structure of the complex between cyclophilin and cyclosporin A is predicted by combining X-ray crystallographic and NMR spectroscopic data using molecular modeling. The drug was placed at the receptor site using a directed docking procedure in which an impulse is imparted to a pre-oriented ligand along an established path. Both ligand and receptor atoms are flexible during the procedure. Two conformers of the MeBMT side chain are shown to result in similar ligand-receptor interaction energies. The models for the drug-receptor complex appear consistent with known experimental data and provide a significant opportunity for the design of compounds with enhanced therapeutic value.
authors.affiliation: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
authors.forename: S
authors.initials: S
authors.lastname: Gallion
authors.forename: D
authors.initials: D
authors.lastname: Ringe
mesh_terms: D000591:Amino Acid Isomerases / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D016572:Cyclosporine / Q000737:chemistry*; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D011971:Receptors, Immunologic / Q000737:chemistry*
chemical_list: D002352:Carrier Proteins; D046911:Macromolecular Substances; D011971:Receptors, Immunologic; C028752:cyclosporin receptor; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase