Abstract
Background: Bcl-XL binds Bax at mitochondria, inhibiting Bax oligomerization and apoptosis. Results: Anchored in membranes, Bcl-XL•Bax heterodimer is formed from a rigid helix-in-groove interface plus a flexible helical dimer interface. Conclusion: Two interfaces contribute equally to the heterodimer stability required to inhibit Bax. Significance: This novel kind of protein-protein interaction stabilizes the membrane-bound heterodimer that is pivotal to apoptosis regulation.
Original language | English (US) |
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Pages (from-to) | 11873-11896 |
Number of pages | 24 |
Journal | Journal of Biological Chemistry |
Volume | 289 |
Issue number | 17 |
DOIs | |
State | Published - Apr 25 2014 |