6X8O
BimBH3 peptide tetramer
Summary for 6X8O
| Entry DOI | 10.2210/pdb6x8o/pdb |
| Descriptor | Bcl-2-like protein 11, THIOCYANATE ION (3 entities in total) |
| Functional Keywords | bim, cell death, bcl-2, bh3, apoptosis |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 13148.87 |
| Authors | Robin, A.Y.,Westphal, D.,Uson, I.,Czabotar, P.E. (deposition date: 2020-06-01, release date: 2020-09-09, Last modification date: 2024-10-09) |
| Primary citation | Assafa, T.E.,Nandi, S.,Smilowicz, D.,Galazzo, L.,Teucher, M.,Elsner, C.,Putz, S.,Bleicken, S.,Robin, A.Y.,Westphal, D.,Uson, I.,Stoll, R.,Czabotar, P.E.,Metzler-Nolte, N.,Bordignon, E. Biophysical Characterization of Pro-apoptotic BimBH3 Peptides Reveals an Unexpected Capacity for Self-Association. Structure, 29:114-124.e3, 2021 Cited by PubMed Abstract: Bcl-2 proteins orchestrate the mitochondrial pathway of apoptosis, pivotal for cell death. Yet, the structural details of the conformational changes of pro- and antiapoptotic proteins and their interactions remain unclear. Pulse dipolar spectroscopy (double electron-electron resonance [DEER], also known as PELDOR) in combination with spin-labeled apoptotic Bcl-2 proteins unveils conformational changes and interactions of each protein player via detection of intra- and inter-protein distances. Here, we present the synthesis and characterization of pro-apoptotic BimBH3 peptides of different lengths carrying cysteines for labeling with nitroxide or gadolinium spin probes. We show by DEER that the length of the peptides modulates their homo-interactions in the absence of other Bcl-2 proteins and solve by X-ray crystallography the structure of a BimBH3 tetramer, revealing the molecular details of the inter-peptide interactions. Finally, we prove that using orthogonal labels and three-channel DEER we can disentangle the Bim-Bim, Bcl-xL-Bcl-xL, and Bim-Bcl-xL interactions in a simplified interactome. PubMed: 32966763DOI: 10.1016/j.str.2020.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.31 Å) |
Structure validation
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