Conformation of two non‐immunosuppressive FK506 analogs when bound to FKBP by isotope‐filtered NMR
- 24 August 1992
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 308 (3) , 309-314
- https://doi.org/10.1016/0014-5793(92)81300-b
Abstract
The 3D structure of two unlabeled FK506 analogs, (R)‐ and (S)‐[18‐OH]ascomycin, when bound to [U‐13C,14N]FKBP were determined by isotope‐filtered 2D NMR experiments. The structures for the R and S isomers that bind tightly to FKBP but lack immunosuppresive activity are compared to each other and to the conformation of the potent immunosuppressant, ascomycin, when bound to FKBP. The results are interpreted in terms of calcineurin binding to the FKBP/ascomycin complex.Keywords
This publication has 20 references indexed in Scilit:
- Determination of three‐dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms Circumventing problems associated with foldingPublished by Wiley ,2001
- An improved method for selectively observing protons attached to 12C in the presence of 1H13C spin pairsJournal of Magnetic Resonance (1969), 1992
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexesCell, 1991
- A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomeraseNature, 1989
- A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilinNature, 1989
- Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier proteinFEBS Letters, 1989
- Determining stereo-specific 1H nuclear magnetic resonance assignments from distance geometry calculationsJournal of Molecular Biology, 1988
- Editing of 2D 1H NMR spectra using X half-filters. combined use with residue-selective 15N labeling of proteinsJournal of Magnetic Resonance (1969), 1986
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983