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 3.45&Aring;" /> '''Bcl-XL 3D Domain Sw...)
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'''Bcl-XL 3D Domain Swapped Dimer'''<br />
'''Bcl-XL 3D Domain Swapped Dimer'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B48 OCA].
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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]]
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[[Category: Hockenbery, D.M.]]
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[[Category: Hockenbery, D M.]]
[[Category: Maguire, B.]]
[[Category: Maguire, B.]]
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[[Category: Manion, M.K.]]
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[[Category: Manion, M K.]]
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[[Category: Neill, J.W.O.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:58:15 2007''
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''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


2b48, resolution 3.45Å

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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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