Solution structure of FK506 bound to FKBP-12

• Published in: FEBS letters Vol. 302; no. 1; pp. 89 - 96
• Main Authors: Lepre, Christopher A., Thomson, John A., Moore, Jonathan M.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 04.05.1992; Elsevier
• Subjects: Biological and medical sciences; Carrier Proteins - chemistry; Carrier Proteins - metabolism; correlated spectroscopy; COSY; CsA; cyclophilin; cyclosporin A; CyP; distance geometry; double quantum; double quantum filtered; DQF; FK506; FK506 binding protein (11.8 kDa); FKBP; FKBP-12; GARP; globally optimized alternating-phase rectangular pulses; heteronuclear multiple quantum coherence spectroscopy; heteronuclear single quantum coherence spectroscopy; heteronuclear single quantum coherence-nuclear Overhauser enhancement spectroscopy; HMQC; hrFKBP-12; HSQC; HSQC-NOESY; human recombinant FKBP-12; Immunomodulators; Immunophilin; Magnetic Resonance Spectroscopy; Medical sciences; Models, Molecular; Molecular Conformation; molecular dynamics; Molecular Structure; NMR; NOE; NOESY; nuclear magnetic resonance; nuclear Overhauser enhancement; Peptidyl-prolyl cis-trans isomerase; Pharmacology. Drug treatments; Solutions; Tacrolimus - chemistry; Tacrolimus - metabolism; Tacrolimus Binding Proteins; TOCSY; total correlation spectroscopy; two dimensional; two-dimensional NOE spectroscopy; Peptidyl-prolyl cis-trans isomerase; DG; NOE; HSQC-NOESY; TOCSY; FK506; COSY; DQ; FKBP-12; CsA; NMR; 2D; FKBP; HMQC; MD; DQF; hrFKBP-12; GARP; NOESY; CyP; HSQC; Immunophilin; Signal transduction; Enzyme; Overhauser effect; NMR spectrometry; Method; Isomerase; Structural analysis

The complex of the immunosuppressant FK506 bound to FKBP-12 has been studied in solution using 1H and inverse-detected 13C NMR methods. The resonances of bound, 13C-labelled FK506 were assigned and a set of 66 intraligand NOE distance restraints were used to calculate the structure of the bound liga...