2b48
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(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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Revision as of 18:51, 12 November 2007
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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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