title: The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A.
abstract: Human cyclophilin A (165 residues) has peptidyl-prolyl cis-trans isomerase activity. Here we report a high-resolution three-dimensional X-ray structure of a substrate, ac-Ala-Ala-Pro-Ala-amc (ac, acetyl; amc, amidomethylcoumarin) bound to the active-site of cyclophilin. The structure consisting of a dimer of complexes and 135 water molecules was refined to a crystallographic R-factor of 17.7% for all data in the range 8 A-2.3 A.
authors.affiliation: Preclinical Research, Sandoz Pharma AG, Basel, Switzerland.
authors.forename: J
authors.initials: J
authors.lastname: Kallen
authors.forename: M D
authors.initials: MD
authors.lastname: Walkinshaw
mesh_terms: D000591:Amino Acid Isomerases / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D003524:Cyclosporins / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D019696:Peptidylprolyl Isomerase; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014961:X-Ray Diffraction
chemical_list: D002352:Carrier Proteins; D003524:Cyclosporins; D010455:Peptides; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase