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Structure paper

TitleA PROSS-designed extensively mutated estrogen receptor alpha variant displays enhanced thermal stability while retaining native allosteric regulation and structure.
Journal, issue, pagesSci Rep, Vol. 11, Page 10509-10509, Year 2021
Publish dateFeb 2, 2021 (structure data deposition date)
AuthorsKriegel, M. / Wiederanders, H.J. / Alkhashrom, S. / Eichler, J. / Muller, Y.A.
External linksSci Rep / PubMed:34006920
MethodsX-ray diffraction
Resolution1.33 - 1.6 Å
Structure data

PDB-7ndo:
ER-PRS*(-) (L536S, L372R) in complex with raloxifene
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-7nel:
ER-PRS*(+) (Y537S) in complex with estradiol and SRC-2 coactivator peptide
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-7nfb:
ER-PRS*(+) (Y537S) in complex with genistein and SRC-2 coactivator peptide
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

Chemicals

ChemComp-RAL:
RALOXIFENE / medication*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-EST:
ESTRADIOL / hormone*YM

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-GEN:
GENISTEIN / inhibitor*YM

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / human estrogen receptor alpha / hERa-LBD / raloxifene / ligand binding domain / ER / estradiol / SRC-2 / genistein

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