RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination
Leo Kiss, Dean Clift, Nadine Renner and 2 more
Nature Communications · 2021
doi:10.1038/s41467-021-21443-6 (opens in a new tab)
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Abstract
The mechanism by which RING E3-anchored ubiquitin chains are formed is not well understood. Here, the authors solve a crystal structure of the RING E3 enzyme TRIM21 trapped in the process of self-anchored chain elongation and provide biochemical and cellular insights into the mechanism of ubiquitin conjugation.
Abstract licence: CC BY-NC-ND
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