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Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation

Commun Biol. 2021-04; 
Ameeq Ul Mushtaq, Jörgen Ådén, Luke A Clifton, Hanna Wacklin-Knecht, Mario Campana, Artur P G Dingeldein, Cecilia Persson, Tobias Sparrman, Gerhard Gröbner
Products/Services Used Details Operation
Custom Vector Construction A glycerol stock of transformed BL21(DE3) Rosetta™ cells with Bcl-2 encoded in a pET-15b vector (Novagen) was ordered from GenScript (Leiden, Netherlands) Get A Quote

摘要

B-cell lymphoma 2 (Bcl-2) proteins are the main regulators of mitochondrial apoptosis. Anti-apoptotic Bcl-2 proteins possess a hydrophobic tail-anchor enabling them to translocate to their target membrane and to shift into an active conformation where they inhibit pro-apoptotic Bcl-2 proteins to ensure cell survival. To address the unknown molecular basis of their cell-protecting functionality, we used intact human Bcl-2 protein natively residing at the mitochondrial outer membrane and applied neutron reflectometry and NMR spectroscopy. Here we show that the active full-length protein is entirely buried into its target membrane except for the regulatory flexible loop domain (FLD), which stretches into the aqueo... More

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