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Structural analysis of the LDL receptor-interacting FERM domain in the E3 ubiquitin ligase IDOL reveals an obscured substrate-binding site

Research output: Contribution to journal › Article › Academic › peer-review

DOI

https://doi.org/10.1074/jbc.RA120.014349
Final published version

Luca Martinelli
Athanassios Adamopoulos
Patrik Johansson
Paul T. Wan
Jenny Gunnarsson
Hongwei Guo
Helen Boyd
Noam Zelcer
Titia K. Sixma

Original language	English
Pages (from-to)	13570-13583
Number of pages	14
Journal	Journal of biological chemistry
Volume	295
Issue number	39
DOIs	https://doi.org/10.1074/jbc.RA120.014349
Publication status	Published - 25 Sept 2020

Research areas

E3 ubiquitin ligase, FERM, FERM domain, IDOL, LDL receptor, LDLR, MYLIP, cholesterol metabolism, crystal structure, enzyme purification, lipoprotein metabolism, low-density lipoprotein (LDL), protein structure, small-angle X-ray scattering (SAXS), ubiquitylation (ubiquitination)

ID: 13542153