2B48
Bcl-XL 3D Domain Swapped Dimer
Summary for 2B48
| Entry DOI | 10.2210/pdb2b48/pdb |
| Related | 1MAZ 1R2D |
| Descriptor | Apoptosis regulator Bcl-X (1 entity in total) |
| Functional Keywords | apoptosis, dimeric, 3d domain swap, alpha-helical, apoptosis inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817 |
| Total number of polymer chains | 1 |
| Total formula weight | 24606.94 |
| Authors | O'Neill, J.W.,Manion, M.K.,Maguire, B.,Hockenbery, D.M. (deposition date: 2005-09-22, release date: 2006-02-14, Last modification date: 2023-08-23) |
| Primary citation | O'Neill, J.W.,Manion, M.K.,Maguire, B.,Hockenbery, D.M. BCL-X(L) Dimerization by Three-dimensional Domain Swapping. J.Mol.Biol., 356:367-381, 2006 Cited by PubMed Abstract: Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 protein family are dynamically regulated and intimately involved in survival and death functions. We report the structure of a BCL-X(L) homodimers a 3D-domain swapped dimer (3DDS). The X-ray crystal structure demonstrates the mutual exchange of carboxy-terminal regions including BH2 (Bcl-2 homology 2) between monomer subunits, with the hinge region occurring at the hairpin turn between the fifth and sixth alpha helices. Both BH3 peptide-binding hydrophobic grooves are unoccupied in the 3DDS dimer and available for BH3 peptide binding, as confirmed by sedimentation velocity analysis. BCL-X(L) 3DDS dimers have increased pore-forming activity compared to monomers, suggesting that 3DDS dimers may act as intermediates in membrane pore formation. Chemical crosslinking studies of Cys-substituted BCL-X(L) proteins demonstrate that 3DDS dimers form in synthetic lipid vesicles. PubMed: 16368107DOI: 10.1016/j.jmb.2005.11.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.45 Å) |
Structure validation
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