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Structure paper

TitleCrystal Structures of the Free and Ligand-Bound FK1-FK2 Domain Segment of FKBP52 Reveal a Flexible Inter-Domain Hinge.
Journal, issue, pagesJ. Mol. Biol., Vol. 425, Page 4134-4144, Year 2013
Publish dateJun 20, 2013 (structure data deposition date)
AuthorsBracher, A. / Kozany, C. / Hahle, A. / Wild, P. / Zacharias, M. / Hausch, F.
External linksJ. Mol. Biol. / PubMed:23933011
MethodsX-ray diffraction
Resolution1.7 - 2.4 Å
Structure data

PDB-4lav:
Crystal Structure Analysis of FKBP52, Crystal Form II
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4law:
Crystal Structure Analysis of FKBP52, Crystal Form III
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4lax:
Crystal Structure Analysis of FKBP52, Complex with FK506
Method: X-RAY DIFFRACTION / Resolution: 2.007 Å

PDB-4lay:
Crystal Structure Analysis of FKBP52, Complex with I63
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-FK5:
8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN / medication*YM

ChemComp-GOL:
GLYCEROL

ChemComp-I63:
{3-[(1R)-3-(3,4-dimethoxyphenyl)-1-({[(2S)-1-(3,3-dimethyl-2-oxopentanoyl)piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic acid

Source
  • homo sapiens (human)
KeywordsISOMERASE / Fk-506 binding domain / Hsp90 cochaperone / immunophilin / peptidyl-prolyl isomerase / protein folding

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