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TitleStructural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate-binding site.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 13570-13583, Year 2020
Publish dateFeb 1, 2019 (structure data deposition date)
AuthorsMartinelli, L. / Adamopoulos, A. / Johansson, P. / Wan, P.T. / Gunnarsson, J. / Guo, H. / Boyd, H. / Zelcer, N. / Sixma, T.K.
External linksJ. Biol. Chem. / PubMed:32727844
MethodsX-ray diffraction
Resolution2.343 - 2.5 Å
Structure data

PDB-6qly:
IDOL FERM domain
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6qlz:
IDOL F3ab subdomain
Method: X-RAY DIFFRACTION / Resolution: 2.343 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / FERM domain; Ubiquitin E3 LIGASE CHOLESTEROL METABOLISM / LDLR degradation / E3 LIGASE CHOLESTEROL METABOLISM LDLR degradation

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