Elucidation of some Bax conformational changes through crystallization of an antibody–peptide complex
Copyright policy )Elucidation of some Bax conformational changes through crystallization of an antibody–peptide complex
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.
- National Jewish Health United States
- University of New Mexico Hospital United States
- Howard Hughes Medical Institute United States
- University of Colorado Health United States
- University of Colorado Cancer Center United States
Models, Molecular, Binding Sites, Protein Conformation, Antibodies, Protein Structure, Tertiary, Epitopes, Immunoglobulin Fab Fragments, Structure-Activity Relationship, Cell Line, Tumor, Humans, Crystallization, Peptides, Protein Binding, bcl-2-Associated X Protein
Models, Molecular, Binding Sites, Protein Conformation, Antibodies, Protein Structure, Tertiary, Epitopes, Immunoglobulin Fab Fragments, Structure-Activity Relationship, Cell Line, Tumor, Humans, Crystallization, Peptides, Protein Binding, bcl-2-Associated X Protein
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