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

Autor: 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
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-019-10363-1
Popis: 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.
Databáze: Directory of Open Access Journals