1R2D: Structure Of Human Bcl-xl At 1.95 Angstroms

Citation:
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.
PDB ID: 1R2DDownload
MMDB ID: 26149
PDB Deposition Date: 2003/9/26
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Similar Structures:
Biological Unit for 1R2D: monomeric; determined by author
Molecular Components in 1R2D
Label Count Molecule
Protein (1 molecule)
1
Apoptosis Regulator Bcl-x(Gene symbol: BCL2L1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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