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

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

The BCL-2 mutation G101V reduces venetoclax affinity and confers drug resistance in patients with chronic lymphocytic leukaemia. Here, the authors present crystal structures and biochemical analyses of venetoclax bound to BCL-2 and the G101V mutant, revealing the structural basis for venetoclax resi...

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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/972a06d765d140d0b0bfb95c8133217b
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Sumario:The BCL-2 mutation G101V reduces venetoclax affinity and confers drug resistance in patients with chronic lymphocytic leukaemia. Here, the authors present crystal structures and biochemical analyses of venetoclax bound to BCL-2 and the G101V mutant, revealing the structural basis for venetoclax resistance.

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