2b48
From Proteopedia
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- | [[Image:2b48.gif|left|200px]] | + | [[Image:2b48.gif|left|200px]] |
- | + | ||
- | '''Bcl-XL 3D Domain Swapped Dimer''' | + | {{Structure |
+ | |PDB= 2b48 |SIZE=350|CAPTION= <scene name='initialview01'>2b48</scene>, resolution 3.45Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= BCL2L1, BCL2L, BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Bcl-XL 3D Domain Swapped Dimer''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2B48 is a [ | + | 2B48 is a [[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== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16368107 16368107] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dimeric]] | [[Category: dimeric]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:22 2008'' |
Revision as of 13:57, 20 March 2008
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, resolution 3.45Å | |||||||
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Gene: | BCL2L1, BCL2L, BCLX (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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