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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/972a06d765d140d0b0bfb95c8133217b
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spelling	oai:doaj.org-article:972a06d765d140d0b0bfb95c8133217b2021-12-02T17:01:53ZStructures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations10.1038/s41467-019-10363-12041-1723https://doaj.org/article/972a06d765d140d0b0bfb95c8133217b2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10363-1https://doaj.org/toc/2041-1723The 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.Richard W. BirkinshawJia-nan GongCindy S. LuoDaisy LioChristine A. WhiteMary Ann AndersonPiers BlomberyGuillaume LesseneIan J. MajewskiRachel ThijssenAndrew W. RobertsDavid C. S. HuangPeter M. ColmanPeter E. CzabotarNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
description	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.
format	article
author	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
author_facet	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
author_sort	Richard W. Birkinshaw
title	Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
title_short	Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
title_full	Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
title_fullStr	Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
title_full_unstemmed	Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations
title_sort	structures of bcl-2 in complex with venetoclax reveal the molecular basis of resistance mutations
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/972a06d765d140d0b0bfb95c8133217b
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Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations

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