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Structure paper

TitleLarge FK506-Binding Proteins Shape the Pharmacology of Rapamycin.
Journal, issue, pagesMol. Cell. Biol., Vol. 33, Page 1357-1367, Year 2013
Publish dateFeb 17, 2012 (structure data deposition date)
AuthorsMarz, A.M. / Fabian, A.K. / Kozany, C. / Bracher, A. / Hausch, F.
External linksMol. Cell. Biol. / PubMed:23358420
MethodsX-ray diffraction
Resolution1.45 - 2.3 Å
Structure data

PDB-4drh:
Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of mTOR at low pH
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4dri:
Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of mTOR
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-4drj:
o-crystal structure of the PPIase domain of FKBP52, Rapamycin and the FRB fragment of mTOR
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-RAP:
RAPAMYCIN IMMUNOSUPPRESSANT DRUG / immunosuppressant, antibiotic*YM

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsIsomerase/Transferase / Fk-506 binding domain / Hsp90 cochaperone / immunophilin / peptidyl-prolyl isomerase / mammalian target of Rapamycin / kinase / signalling / immunosuppression / cancer / Isomerase-Transferase complex

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