Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations

Richard W. Birkinshaw, Jia nan Gong, Cindy S. Luo, Daisy Lio, Christine A. White, Mary Ann Anderson, Piers Blombery, Guillaume Lessene, Ian J. Majewski, Rachel Thijssen, Andrew W. Roberts, David C.S. Huang, Peter M. Colman, Peter E. Czabotar

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Abstract

Venetoclax is a first-in-class cancer therapy that interacts with the cellular apoptotic machinery promoting apoptosis. Treatment of patients suffering chronic lymphocytic leukaemia with this BCL-2 antagonist has revealed emergence of a drug-selected BCL-2 mutation (G101V) in some patients failing therapy. To understand the molecular basis of this acquired resistance we describe the crystal structures of venetoclax bound to both BCL-2 and the G101V mutant. The pose of venetoclax in its binding site on BCL-2 reveals small but unexpected differences as compared to published structures of complexes with venetoclax analogues. The G101V mutant complex structure and mutant binding assays reveal that resistance is acquired by a knock-on effect of V101 on an adjacent residue, E152, with venetoclax binding restored by a E152A mutation. This provides a framework for considering analogues of venetoclax that might be effective in combating this mutation.

Original languageEnglish
Article number2385
JournalNature communications
Volume10
Issue number1
DOIs
Publication statusPublished - 1 Dec 2019

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