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

Nat Commun. 2019-06; 
BirkinshawRichard W,GongJia-Nan,LuoCindy S,LioDaisy,WhiteChristine A,AndersonMary Ann,BlomberyPiers,LesseneGuillaume,MajewskiIan J,ThijssenRachel,RobertsAndrew W,HuangDavid C S,ColmanPeter M,CzabotarPet
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Proteins, Expression, Isolation and Analysis Recombinant GST-BCL-2 fusions were purified from cellular proteins by glutathione-agarase resin (GenScript; CAT#L00206) and eluted with 10 mM reduced glutathione. Get A Quote

摘要

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 acq... More

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