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Structure paper

TitleUnexpected Allosteric Network Contributes to LRH-1 Co-regulator Selectivity.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 1411-1426, Year 2016
Publish dateMay 16, 2014 (structure data deposition date)
AuthorsMusille, P.M. / Kossmann, B.R. / Kohn, J.A. / Ivanov, I. / Ortlund, E.A.
External linksJ. Biol. Chem. / PubMed:26553876
MethodsX-ray diffraction
Resolution1.75 - 1.752 Å
Structure data

PDB-4pld:
Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, in its apo State Bound to a Fragment of Human TIF-2
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4ple:
Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, Bound to an E. Coli Phospholipid and a Fragment of TIF-2
Method: X-RAY DIFFRACTION / Resolution: 1.752 Å

Chemicals

ChemComp-CPS:
3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE / detergent*YM

ChemComp-HOH:
WATER

ChemComp-EPH:
L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / Nuclear Receptor / apo / phospholipid

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