Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acid

@inproceedings{Gopalakrishnan2012ExplorationOP,
  title={Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acid},
  author={R. Gopalakrishnan and C. Kozany and Y. Wang and B. Hoogeland and A. Bracher and F. Hausch and S. Schneider},
  year={2012}
}
3 Citations
Discovery of pentapeptide-inhibitor hits targeting FKBP51 by combining computational modeling and X-ray crystallography
  • Jian-Ting Han, Yongchang Zhu, +6 authors Xiaojun Yao
  • Medicine
  • Computational and structural biotechnology journal
  • 2021
Graphical abstract Peptide-inhibitor hits were designed with small molecules published before used as the starting point through structure-based drug design and biochemically and structurallyExpand
A β-Turn Motif in the Steroid Hormone Receptor's Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52.
TLDR
The crystal structure of human estrogen receptor α and using nuclear magnetic resonance, it is shown that the short V(364)PGF(367) sequence, which is located within its ligand-binding domain and adopts a type II β-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52. Expand
Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands
  • A. Galat
  • Biology, Medicine
  • Cellular and Molecular Life Sciences
  • 2012
From 5 to 12 FK506-binding proteins (FKBPs) are encoded in the genomes of disparate marine organisms, which appeared at the dawn of evolutionary events giving rise to primordial multicellularExpand