1r2e: Difference between revisions

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[[Image:1r2e.gif|left|200px]]
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[[Image:1r2e.png|left|200px]]


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{{STRUCTURE_1r2e|  PDB=1r2e  |  SCENE=  }}  
{{STRUCTURE_1r2e|  PDB=1r2e  |  SCENE=  }}  


'''Human Bcl-XL containing a Glu to Leu mutation at position 92'''
===Human Bcl-XL containing a Glu to Leu mutation at position 92===




==Overview==
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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.
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{{ABSTRACT_PUBMED_14534311}}


==About this Structure==
==About this Structure==
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[[Category: Monomeric]]
[[Category: Monomeric]]
[[Category: Mutation]]
[[Category: Mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:52:10 2008''

Revision as of 12:52, 28 July 2008

File:1r2e.png

Template:STRUCTURE 1r2e

Human Bcl-XL containing a Glu to Leu mutation at position 92

Template:ABSTRACT PUBMED 14534311

About this Structure

1R2E 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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