1r2h | pdb_00001r2h

Human Bcl-XL containing an Ala to Leu mutation at position 142

spinqualitylabelsall models 1r2h, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r2h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1maz, 1r2d, 1r2e, 1r2g, 1r2i Gene: BCL-XL (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Bcl-XL mutations suppress cellular sensitivity to antimycin A.,Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM J Biol Chem. 2004 Jan 16;279(3):2159-65. Epub 2003 Oct 8. PMID:14534311 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bcl-2

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