Fig. 3: The mechanism of RING-anchored ubiquitination in trans. | Nature Communications

Fig. 3: The mechanism of RING-anchored ubiquitination in trans.

From: RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination

Fig. 3

a Surface representation of the canonical model of the Ub-R:Ube2N~Ub:Ube2V2 structure (Ub-R, Ub in red, R in blue, Ube2N~Ub, Ube2N in green, Ub in orange, and Ube2V2 in teal). b Domain architecture of TRIM21 constructs used in biochemical assays. c Cartoon models of substrate (Fc, gray) engagement by TRIM21 constructs (blue). The structural basis for these models is shown in Supplementary Fig. 8. d Substrate (Fc)-induced self-ubiquitination assay of 100 nM Ub-TRIM21 constructs. Reactions were incubated for 5 min at 37 °C. Further data can be found in Supplementary Fig. 9. * (asterisk) indicates a TRIM21 degradation product that could not be removed during purification. Western blots are representative of n = 3 independently performed experiments. Uncropped blots are provided in Source data. Ub ubiquitin, R RING, B Box, CC coiled-coil, PS PRYSPRY, kDa kilo Dalton.

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