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In the absence of BTK-directed therapies, however, cells bearing BTKA428D exhibited a competitive disadvantage. A crystal structure of BTKA428D revealed that the mutant aspartate clashes with the adenine ring of adenosine triphosphate and the adenine-mimetic moiety of BTK inhibitors and degraders. Combining BTK degraders with venetoclax mitigated the expansion of BTKA428D. These results provide the molecular basis for clinical resistance to BTK degraders and will inform the development of next-generation BTK degrader therapies.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>BTK degraders are a promising new therapy for CLL. We demonstrate that BTKA428D is a recurrent BTK degrader resistance mutation in patients that confers pan-resistance to BTK inhibitors and degraders due to steric clash with their shared, adenine-mimetic moiety. 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