Conformational Entropy of FK506 Binding to FKBP12 Determined by Nuclear Magnetic Resonance Relaxation and Molecular Dynamics Simulations
Author:
Affiliation:
1. Biophysical Chemistry, Center for Molecular Protein Science, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden
Funder
Vetenskapsr?det
G?ran Gustafssons Stiftelse f?r Naturvetenskaplig och Medicinsk Forskning
Knut och Alice Wallenbergs Stiftelse
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b01256
Reference93 articles.
1. Rapamycin (AY-22,989), a new antifungal antibiotic. I. Taxonomy of the producing streptomycete and isolation of the active principle.
2. FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics.
3. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
4. Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin.
5. Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein
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