1pq0

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{{Seed}}
 
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[[Image:1pq0.png|left|200px]]
 
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==Crystal structure of mouse Bcl-xl==
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The line below this paragraph, containing "STRUCTURE_1pq0", creates the "Structure Box" on the page.
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<StructureSection load='1pq0' size='340' side='right'caption='[[1pq0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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{{STRUCTURE_1pq0| PDB=1pq0 | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/1pq0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pq0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of mouse Bcl-xl===
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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<ref>PMID:14499110</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1pq0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_14499110}}, adds the Publication Abstract to the page
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 14499110 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14499110}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1PQ0 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14499110 14499110]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Dai S]]
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[[Category: Dai, S.]]
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[[Category: Kappler JW]]
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[[Category: Kappler, J W.]]
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[[Category: Liu X]]
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[[Category: Liu, X.]]
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[[Category: Marrack P]]
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[[Category: Marrack, P.]]
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[[Category: Zhu Y]]
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[[Category: Zhu, Y.]]
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[[Category: Bcl-xl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:24:18 2008''
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Current revision

Crystal structure of mouse Bcl-xl

PDB ID 1pq0

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