1r2h: Difference between revisions

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[[Image:1r2h.gif|left|200px]]
{{Seed}}
[[Image:1r2h.png|left|200px]]


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{{STRUCTURE_1r2h|  PDB=1r2h  |  SCENE=  }}  
{{STRUCTURE_1r2h|  PDB=1r2h  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_14534311}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14534311 is the PubMed ID number.
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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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