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From Proteopedia
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==Crystal structure of Bcl-2 in complex with HBx-BH3 motif== | ==Crystal structure of Bcl-2 in complex with HBx-BH3 motif== | ||
<StructureSection load='5fcg' size='340' side='right' caption='[[5fcg]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5fcg' size='340' side='right' caption='[[5fcg]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/E9L5H4_HBV E9L5H4_HBV]] Multifunctional protein that may modulate protein degradation pathways, apoptosis, transcription, signal transduction, cell cycle progress, and genetic stability by directly or indirectly interacting with host factors.[RuleBase:RU361181] | [[http://www.uniprot.org/uniprot/E9L5H4_HBV E9L5H4_HBV]] Multifunctional protein that may modulate protein degradation pathways, apoptosis, transcription, signal transduction, cell cycle progress, and genetic stability by directly or indirectly interacting with host factors.[RuleBase:RU361181] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | HBx is a hepatitis B virus protein that is required for viral infectivity and replication. Anti-apoptotic Bcl-2 family members are thought to be among the important host targets of HBx. However, the structure and function of HBx are poorly understood and the molecular mechanism of HBx-induced carcinogenesis remains unknown. In this study, we report biochemical and structural characterization of HBx. The recombinant HBx protein contains metal ions, in particular iron and zinc. A BH3-like motif in HBx (residues 110-135) binds Bcl-2 with a dissociation constant of approximately 193 muM, which is drastically lower than that for a canonical BH3 motif from Bim or Bad. Structural analysis reveals that, similar to other BH3 motifs, the BH3-like motif of HBx adopts an amphipathic alpha-helix and binds the conserved BH3-binding groove on Bcl-2. Unlike the helical Bim or Bad BH3 motif, the C-terminal portion of the bound HBx BH3-like motif has an extended conformation and makes considerably fewer interactions with Bcl-2. These observations suggest that HBx may modulate Bcl-2 function in a way that is different from that of the classical BH3-only proteins. | ||
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| + | Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx.,Jiang T, Liu M, Wu J, Shi Y Proc Natl Acad Sci U S A. 2016 Feb 23;113(8):2074-9. doi:, 10.1073/pnas.1525616113. Epub 2016 Feb 8. PMID:26858413<ref>PMID:26858413</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5fcg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:08, 26 February 2016
Crystal structure of Bcl-2 in complex with HBx-BH3 motif
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Categories: Jiang, T Y | Liu, M H | Shi, Y G | Wu, J P | Apoptosis | Complex
