2b48
From Proteopedia
(New page: 200px<br /> <applet load="2b48" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b48, resolution 3.45Å" /> '''Bcl-XL 3D Domain Sw...) |
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- | [[Image:2b48.gif|left|200px]]<br /> | + | [[Image:2b48.gif|left|200px]]<br /><applet load="2b48" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="2b48" size=" | + | |
caption="2b48, resolution 3.45Å" /> | caption="2b48, resolution 3.45Å" /> | ||
'''Bcl-XL 3D Domain Swapped Dimer'''<br /> | '''Bcl-XL 3D Domain Swapped Dimer'''<br /> | ||
==Overview== | ==Overview== | ||
- | Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 | + | Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 protein family are dynamically regulated and intimately involved in survival and death functions. We report the structure of a BCL-X(L) homodimers a 3D-domain swapped dimer (3DDS). The X-ray crystal structure demonstrates the mutual exchange of carboxy-terminal regions including BH2 (Bcl-2 homology 2) between monomer subunits, with the hinge region occurring at the hairpin turn between the fifth and sixth alpha helices. Both BH3 peptide-binding hydrophobic grooves are unoccupied in the 3DDS dimer and available for BH3 peptide binding, as confirmed by sedimentation velocity analysis. BCL-X(L) 3DDS dimers have increased pore-forming activity compared to monomers, suggesting that 3DDS dimers may act as intermediates in membrane pore formation. Chemical crosslinking studies of Cys-substituted BCL-X(L) proteins demonstrate that 3DDS dimers form in synthetic lipid vesicles. |
==About this Structure== | ==About this Structure== | ||
- | 2B48 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:// | + | 2B48 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=2B48 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Hockenbery, D | + | [[Category: Hockenbery, D M.]] |
[[Category: Maguire, B.]] | [[Category: Maguire, B.]] | ||
- | [[Category: Manion, M | + | [[Category: Manion, M K.]] |
- | [[Category: Neill, J | + | [[Category: Neill, J W.O.]] |
[[Category: 3d domain swap]] | [[Category: 3d domain swap]] | ||
[[Category: alpha-helical]] | [[Category: alpha-helical]] | ||
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[[Category: dimeric]] | [[Category: dimeric]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:58 2008'' |
Revision as of 14:34, 21 February 2008
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Bcl-XL 3D Domain Swapped Dimer
Overview
Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 protein family are dynamically regulated and intimately involved in survival and death functions. We report the structure of a BCL-X(L) homodimers a 3D-domain swapped dimer (3DDS). The X-ray crystal structure demonstrates the mutual exchange of carboxy-terminal regions including BH2 (Bcl-2 homology 2) between monomer subunits, with the hinge region occurring at the hairpin turn between the fifth and sixth alpha helices. Both BH3 peptide-binding hydrophobic grooves are unoccupied in the 3DDS dimer and available for BH3 peptide binding, as confirmed by sedimentation velocity analysis. BCL-X(L) 3DDS dimers have increased pore-forming activity compared to monomers, suggesting that 3DDS dimers may act as intermediates in membrane pore formation. Chemical crosslinking studies of Cys-substituted BCL-X(L) proteins demonstrate that 3DDS dimers form in synthetic lipid vesicles.
About this Structure
2B48 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
BCL-XL dimerization by three-dimensional domain swapping., O'Neill JW, Manion MK, Maguire B, Hockenbery DM, J Mol Biol. 2006 Feb 17;356(2):367-81. Epub 2005 Dec 1. PMID:16368107
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