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1r2e
From Proteopedia
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[[Image:1r2e.gif|left|200px]] | [[Image:1r2e.gif|left|200px]] | ||
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'''Human Bcl-XL containing a Glu to Leu mutation at position 92''' | '''Human Bcl-XL containing a Glu to Leu mutation at position 92''' | ||
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[[Category: Neill, J W.O.]] | [[Category: Neill, J W.O.]] | ||
[[Category: Zhang, K Y.]] | [[Category: Zhang, K Y.]] | ||
| - | [[Category: | + | [[Category: Alpha-helical]] |
| - | [[Category: | + | [[Category: Apoptosis]] |
| - | [[Category: | + | [[Category: Monomeric]] |
| - | [[Category: | + | [[Category: Mutation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:59:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:59, 3 May 2008
Human Bcl-XL containing a Glu to Leu mutation at position 92
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
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 Page seeded by OCA on Sat May 3 06:59:31 2008
