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| | ==Crystal structure of mouse Bcl-xl== | | ==Crystal structure of mouse Bcl-xl== |
| - | <StructureSection load='1pq0' size='340' side='right' caption='[[1pq0]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1pq0' size='340' side='right'caption='[[1pq0]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pq0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PQ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PQ0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pq1|1pq1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2L1 OR BCL2L OR BCLX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1pq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pq0 OCA], [https://pdbe.org/1pq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pq0 RCSB], [https://www.ebi.ac.uk/pdbsum/1pq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pq0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pq0 OCA], [http://pdbe.org/1pq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1pq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pq0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B2CL1_MOUSE B2CL1_MOUSE]] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:9390687</ref> Isoform Bcl-X(S) promotes apoptosis (By similarity).<ref>PMID:9390687</ref> | + | [https://www.uniprot.org/uniprot/B2CL1_MOUSE B2CL1_MOUSE] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:9390687</ref> Isoform Bcl-X(S) promotes apoptosis (By similarity).<ref>PMID:9390687</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1pq0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1pq0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Dai, S]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kappler, J W]] | + | [[Category: Dai S]] |
| - | [[Category: Liu, X]] | + | [[Category: Kappler JW]] |
| - | [[Category: Marrack, P]] | + | [[Category: Liu X]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Marrack P]] |
| - | [[Category: Apoptosis]]
| + | [[Category: Zhu Y]] |
| - | [[Category: Bcl-xl]]
| + | |
| Structural highlights
Function
B2CL1_MOUSE Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.[1] Isoform Bcl-X(S) promotes apoptosis (By similarity).[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
After antigen-driven expansion, the majority of T cells involved in an immune response die rapidly by apoptosis dependent on the Bcl-2 related proteins, Bim and Bax or Bak. The details of how these proteins are activated and interact are still unclear. The crystal structure of mouse Bcl-x(L) bound to a long helical fragment of Bim indicates that the structure of Bim is very different from proteins with a Bcl-2-like fold and may leave the BH3 region of Bim constitutively exposed. Based on the structural homology between Bcl-x(L) and Bax, we predicted that binding of Bim to Bax would require displacement of the Bax penultimate alpha helix. Consistent with this prediction, truncation of this short helix was required for Bim/Bax interaction and led to spontaneous activation of Bax. Our results suggest a way in which both Bim and Bax/Bak might be required for activated T cell apoptosis.
The structure of a Bcl-xL/Bim fragment complex: implications for Bim function.,Liu X, Dai S, Zhu Y, Marrack P, Kappler JW Immunity. 2003 Sep;19(3):341-52. PMID:14499110[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang XF, Weber GF, Cantor H. A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells. Immunity. 1997 Nov;7(5):629-39. PMID:9390687
- ↑ Yang XF, Weber GF, Cantor H. A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells. Immunity. 1997 Nov;7(5):629-39. PMID:9390687
- ↑ Liu X, Dai S, Zhu Y, Marrack P, Kappler JW. The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity. 2003 Sep;19(3):341-52. PMID:14499110
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