1ZY3
Structural model of complex of Bcl-w protein with Bid BH3-peptide
Summary for 1ZY3
| Entry DOI | 10.2210/pdb1zy3/pdb |
| Related | 1mk3 |
| Descriptor | Apoptosis regulator Bcl-W, BH3-peptide from BH3 interacting domain death agonist protein (2 entities in total) |
| Functional Keywords | apoptosis, bcl-w, bh3-peptide |
| Biological source | Homo sapiens (human) More |
| Cellular location | Mitochondrion membrane; Peripheral membrane protein: Q92843 Cytoplasm (By similarity). BH3-interacting domain death agonist p15: Mitochondrion membrane (By similarity). BH3-interacting domain death agonist p13: Mitochondrion membrane (By similarity). Isoform 1: Cytoplasm. Isoform 3: Cytoplasm. Isoform 2: Mitochondrion membrane: P55957 |
| Total number of polymer chains | 2 |
| Total formula weight | 21901.50 |
| Authors | Denisov, A.Y.,Gehring, K. (deposition date: 2005-06-09, release date: 2006-02-14, Last modification date: 2024-05-22) |
| Primary citation | Denisov, A.Y.,Chen, G.,Sprules, T.,Moldoveanu, T.,Beauparlant, P.,Gehring, K. Structural Model of the BCL-w-BID Peptide Complex and Its Interactions with Phospholipid Micelles. Biochemistry, 45:2250-2256, 2006 Cited by PubMed Abstract: A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide. PubMed: 16475813DOI: 10.1021/bi052332s PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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