The structure of a giant ubiquitin E3 ligase sheds light on its activation in a substrate-dependent manner and shows how a single E3 enzyme uses distinct recognition modules to confer substrate specificity.
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References
Mark, K. G. & Rape, M. EMBO Rep. 22, e51078 (2021).
Grabarczyk, D. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-021-00831-5 (2021).
Harper, J. W. & Schulman, B. A. Annu. Rev. Biochem. 90, 403–429 (2021).
Fernandez-Martinez, J. & Rout, M. P. Trends Biochem. Sci. 46, 595–607 (2021).
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Ploegh, H. A giant ubiquitin ligase. Nat Chem Biol 17, 1014–1015 (2021). https://doi.org/10.1038/s41589-021-00860-0
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DOI: https://doi.org/10.1038/s41589-021-00860-0