1r2d

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Image:1r2d.gif

1r2d, resolution 1.95Å

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Structure of Human Bcl-XL at 1.95 Angstroms

Overview

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.

About this Structure

1R2D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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