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1r2g
From Proteopedia
(New page: 200px<br /> <applet load="1r2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2g, resolution 2.70Å" /> '''Human Bcl-XL contai...) |
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| - | [[Image:1r2g.gif|left|200px]]<br /> | + | [[Image:1r2g.gif|left|200px]]<br /><applet load="1r2g" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1r2g" size=" | + | |
caption="1r2g, resolution 2.70Å" /> | caption="1r2g, resolution 2.70Å" /> | ||
'''Human Bcl-XL containing a Phe to Trp mutation at position 97'''<br /> | '''Human Bcl-XL containing a Phe to Trp mutation at position 97'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cells expressing high levels of the BCL-X(L) anti-apoptotic protein are | + | 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== | ==About this Structure== | ||
| - | 1R2G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1R2G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Giedt, C | + | [[Category: Giedt, C D.]] |
| - | [[Category: Hockenbery, D | + | [[Category: Hockenbery, D M.]] |
| - | [[Category: Kim, K | + | [[Category: Kim, K M.]] |
| - | [[Category: Manion, M | + | [[Category: Manion, M K.]] |
| - | [[Category: Neill, J | + | [[Category: Neill, J W.O.]] |
| - | [[Category: Zhang, K | + | [[Category: Zhang, K Y.]] |
[[Category: alpha-helical]] | [[Category: alpha-helical]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
| Line 25: | Line 24: | ||
[[Category: mutation]] | [[Category: mutation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:17 2008'' |
Revision as of 12:46, 21 February 2008
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Human Bcl-XL containing a Phe to Trp mutation at position 97
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
1R2G 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 Thu Feb 21 14:46:17 2008
