2b48

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[[Image:2b48.gif|left|200px]]
[[Image:2b48.gif|left|200px]]
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{{Structure
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|PDB= 2b48 |SIZE=350|CAPTION= <scene name='initialview01'>2b48</scene>, resolution 3.45&Aring;
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The line below this paragraph, containing "STRUCTURE_2b48", creates the "Structure Box" on the page.
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|SITE=
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|GENE= BCL2L1, BCL2L, BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2b48| PDB=2b48 | SCENE= }}
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|RELATEDENTRY=[[1maz|1MAZ]], [[1r2d|1R2D]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b48 OCA], [http://www.ebi.ac.uk/pdbsum/2b48 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b48 RCSB]</span>
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'''Bcl-XL 3D Domain Swapped Dimer'''
'''Bcl-XL 3D Domain Swapped Dimer'''
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[[Category: Neill, J W.O.]]
[[Category: Neill, J W.O.]]
[[Category: 3d domain swap]]
[[Category: 3d domain swap]]
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[[Category: alpha-helical]]
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[[Category: Alpha-helical]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: dimeric]]
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[[Category: Dimeric]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:49:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:12 2008''
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Revision as of 16:49, 3 May 2008

Image:2b48.gif

Template:STRUCTURE 2b48

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 Page seeded by OCA on Sat May 3 19:49:57 2008

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