1R2I
Human Bcl-XL containing a Phe to Leu mutation at position 146
Summary for 1R2I
Entry DOI | 10.2210/pdb1r2i/pdb |
Related | 1MAZ 1R2D 1R2E 1R2G 1R2H |
Descriptor | Apoptosis regulator Bcl-X (2 entities in total) |
Functional Keywords | apoptosis, monomeric, alpha-helical, mutation |
Biological source | Homo sapiens (human) |
Cellular location | Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817 |
Total number of polymer chains | 1 |
Total formula weight | 24572.93 |
Authors | O'Neill, J.W.,Manion, M.K.,Giedt, C.D.,Kim, K.M.,Zhang, K.Y.,Hockenbery, D.M. (deposition date: 2003-09-26, release date: 2004-02-03, Last modification date: 2023-08-23) |
Primary citation | Manion, M.K.,O'Neill, J.W.,Giedt, C.D.,Kim, K.M.,Zhang, K.Y.,Hockenbery, D.M. Bcl-XL mutations suppress cellular sensitivity to antimycin A. J.Biol.Chem., 279:2159-2165, 2004 Cited by PubMed Abstract: Cells expressing high levels of the BCL-X(L) anti-apoptotic protein are preferentially killed by the mitochondrial inhibitor antimycin A (AA). Computational modeling predicts a binding site for AA in the extended hydrophobic groove on BCL-X(L), previously identified as an interface for dimerization to BAX and related proapoptotic proteins. Here, we identify BCL-X(L) hydrophobic groove mutants with normal cellular anti-apoptotic function but suppressed sensitivity to AA. The LD(50) of AA for cells expressing BCL-X(L) mutants directly correlates with the measured in vitro dissociation constants for AA binding. These results indicate that BCL-X(L) is a principal target mediating AA cytotoxicity. PubMed: 14534311DOI: 10.1074/jbc.M306021200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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