2JM6
Solution structure of MCL-1 complexed with NOXAB
Summary for 2JM6
| Entry DOI | 10.2210/pdb2jm6/pdb |
| Related | 1WSX |
| Descriptor | Noxa, Myeloid cell leukemia-1 protein Mcl-1 homolog (2 entities in total) |
| Functional Keywords | apoptosis, mcl-1, bcl-2, helical bundle, bh3-only |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Mitochondrion: Q9JM54 Membrane; Single-pass membrane protein (By similarity): P97287 |
| Total number of polymer chains | 2 |
| Total formula weight | 21405.38 |
| Authors | Czabotar, P.E.,Lee, E.F.,van Delft, M.F.,Day, C.L.,Smith, B.J.,Huang, D.C.S.,Fairlie, W.D.,Hinds, M.G.,Colman, P.M. (deposition date: 2006-10-17, release date: 2007-03-20, Last modification date: 2023-12-20) |
| Primary citation | Czabotar, P.E.,Lee, E.F.,van Delft, M.F.,Day, C.L.,Smith, B.J.,Huang, D.C.S.,Fairlie, W.D.,Hinds, M.G.,Colman, P.M. Structural insights into the degradation of Mcl-1 induced by BH3 domains Proc.Natl.Acad.Sci.Usa, 104:6217-6222, 2007 Cited by PubMed Abstract: Apoptosis is held in check by prosurvival proteins of the Bcl-2 family. The distantly related BH3-only proteins bind to and antagonize them, thereby promoting apoptosis. Whereas binding of the BH3-only protein Noxa to prosurvival Mcl-1 induces Mcl-1 degradation by the proteasome, binding of another BH3-only ligand, Bim, elevates Mcl-1 protein levels. We compared the three-dimensional structures of the complexes formed between BH3 peptides of both Bim and Noxa, and we show that a discrete C-terminal sequence of the Noxa BH3 is necessary to instigate Mcl-1 degradation. PubMed: 17389404DOI: 10.1073/pnas.0701297104 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
