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Here we offer architectural insight into target selection by SCF-FBXL17, a dimerization-quality-control E3 ligase that ubiquitylates and assists to degrade sedentary heterodimers of BTB proteins while sparing useful homodimers. We discover that SCF-FBXL17 disrupts aberrant BTB dimers that fail to support an intermolecular β-sheet around a very divergent β-strand of this BTB domain. Specialized dissociation permits SCF-FBXL17 to wrap around a single BTB domain, resulting in powerful ubiquitylati
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