1r2h
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(New page: 200px<br /> <applet load="1r2h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2h, resolution 2.20Å" /> '''Human Bcl-XL contai...)
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Revision as of 16:52, 12 November 2007
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Human Bcl-XL containing an Ala to Leu mutation at position 142
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
1R2H 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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