Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Bcl-2 family member Bax plays a critical role in apoptosis. In healthy resting cells, Bax resides in the cytoplasm and loosely attached to the mitochondrial membrane. Apoptotic stimuli induce Bax activation, which is characterized by translocation and multimerization on the mitochondrial membrane surface resulting in exposure of an amino terminal epitope recognized by the monoclonal antibody 6A7. To understand the structural changes that occur during Bax activation, we determined the crystal structure of a Bax peptide bound to the 6A7 Fab fragment to a resolution of 2.3 A. The structure reveals the conformation of the 6A7 peptide epitope on Bax in the activated form and elucidates the extensive structural changes that Bax must undergo during the conversion from its native to its activated conformation.
Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex.,Peyerl FW, Dai S, Murphy GA, Crawford F, White J, Marrack P, Kappler JW Cell Death Differ. 2007 Mar;14(3):447-52. Epub 2006 Sep 1. PMID:16946732[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Peyerl FW, Dai S, Murphy GA, Crawford F, White J, Marrack P, Kappler JW. Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex. Cell Death Differ. 2007 Mar;14(3):447-52. Epub 2006 Sep 1. PMID:16946732
