Dataset Information


Conformational Heterogeneity in the Activation Mechanism of Bax.

ABSTRACT: Bax is known for its pro-apoptotic role within the mitochondrial pathway of apoptosis. However, the mechanism for transitioning Bax from cytosolic to membrane-bound oligomer remains elusive. Previous nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) studies defined monomeric Bax as conformationally homogeneous. Yet it has recently been proposed that monomeric Bax exists in equilibrium with a minor state that is distinctly different from its NMR structure. Here, we revisited the structural analysis of Bax using methods uniquely suited for unveiling "invisible" states of proteins, namely, NMR paramagnetic relaxation enhancements and EPR double electron-electron resonance (DEER). Additionally we examined the effect of glycerol, the co-solvent of choice in DEER studies, on the structure of Bax using NMR chemical-shift perturbations and residual dipolar couplings. Based on our combined NMR and EPR results, Bax is a conformationally homogeneous protein prior to its activation.


PROVIDER: S-EPMC5558158 | BioStudies | 2017-01-01

REPOSITORIES: biostudies

Similar Datasets

2016-01-01 | S-EPMC4912045 | BioStudies
2010-01-01 | S-EPMC3057626 | BioStudies
2014-01-01 | S-EPMC4075034 | BioStudies
2017-01-01 | S-EPMC5426344 | BioStudies
2006-01-01 | S-EPMC1635252 | BioStudies
2018-01-01 | S-EPMC6121722 | BioStudies
2016-01-01 | S-EPMC5590656 | BioStudies
1000-01-01 | S-EPMC6108566 | BioStudies
2013-01-01 | S-EPMC3654798 | BioStudies
2019-01-01 | S-EPMC6625747 | BioStudies