3r85

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==Crystal structure of human SOUL BH3 domain in complex with Bcl-xL==
==Crystal structure of human SOUL BH3 domain in complex with Bcl-xL==
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<StructureSection load='3r85' size='340' side='right' caption='[[3r85]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='3r85' size='340' side='right'caption='[[3r85]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r85]] is a 8 chain structure with 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=3R85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R85 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r85]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R85 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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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]] 1.95&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r8j|3r8j]], [[3r8k|3r8k]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3r85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r85 OCA], [https://pdbe.org/3r85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r85 RCSB], [https://www.ebi.ac.uk/pdbsum/3r85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r85 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r85 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r85 RCSB], [http://www.ebi.ac.uk/pdbsum/3r85 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/B2CL1_HUMAN B2CL1_HUMAN] 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:19917720</ref> <ref>PMID:21840391</ref> Isoform Bcl-X(S) promotes apoptosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref>
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== Publication Abstract from PubMed ==
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The SOUL protein is known to induce apoptosis by provoking the mitochondrial permeability transition and a sequence homologous to the Bcl-2 homology 3 (BH3) domains has been recently identified in it thus making it a potential new member of the BH3-only protein family. Here we present NMR, SPR and crystallographic evidence that a peptide spanning SOUL residues 147 - 172 interacts with the anti-apoptotic protein Bcl-xL. We have crystallized SOUL alone and the complex of its BH3 domain peptide with Bcl-xL and solved their three-dimensional structures. The SOUL monomer is a single domain organized as a distorted beta barrel with eight anti-parallel strands and two alpha helices. The BH3 domain extends across 15 residues at the end of the second helix and 8 amino acids in the chain following it. There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.
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Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL.,Ambrosi E, Capaldi S, Bovi M, Saccomani G, Perduca M, Monaco HL Biochem J. 2011 Jun 6. PMID:21639858<ref>PMID:21639858</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ambrosi, E K.]]
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[[Category: Large Structures]]
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[[Category: Bovi, M.]]
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[[Category: Ambrosi EK]]
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[[Category: Capaldi, S.]]
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[[Category: Bovi M]]
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[[Category: Monaco, H L.]]
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[[Category: Capaldi S]]
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[[Category: Perduca, M.]]
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[[Category: Monaco HL]]
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[[Category: Saccomani, G.]]
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[[Category: Perduca M]]
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[[Category: Apoptosis]]
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[[Category: Saccomani G]]
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[[Category: Bcl-2-like protein]]
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[[Category: Inhibitor of cell death]]
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[[Category: Soul protein]]
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Current revision

Crystal structure of human SOUL BH3 domain in complex with Bcl-xL

PDB ID 3r85

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