5fcg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FCG FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcg OCA], [https://pdbe.org/5fcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fcg RCSB], [https://www.ebi.ac.uk/pdbsum/5fcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/BCL2_HUMAN BCL2_HUMAN] Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BCL2_HUMAN BCL2_HUMAN] Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).<ref>PMID:18570871</ref> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5fcg" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Liu | + | ==See Also== |
| - | [[Category: | + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hepatitis B virus]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jiang TY]] | ||
| + | [[Category: Liu MH]] | ||
| + | [[Category: Shi YG]] | ||
| + | [[Category: Wu JP]] | ||
Current revision
Crystal structure of Bcl-2 in complex with HBx-BH3 motif
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Categories: Hepatitis B virus | Homo sapiens | Large Structures | Jiang TY | Liu MH | Shi YG | Wu JP
