This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3r85

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 05:52, 15 June 2022

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

Structural highlights

3r85 is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3r8j, 3r8k
Gene:	BCL2L1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] Isoform Bcl-X(S) promotes apoptosis.^[3] ^[4] [HEBP2_HUMAN] Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.^[5]

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Terrano DT, Upreti M, Chambers TC. Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a functional link coupling mitotic arrest and apoptosis. Mol Cell Biol. 2010 Feb;30(3):640-56. doi: 10.1128/MCB.00882-09. Epub 2009 Nov, 16. PMID:19917720 doi:10.1128/MCB.00882-09
↑ Wang J, Beauchemin M, Bertrand R. Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints. Cell Signal. 2011 Dec;23(12):2030-8. doi: 10.1016/j.cellsig.2011.07.017. Epub, 2011 Aug 5. PMID:21840391 doi:10.1016/j.cellsig.2011.07.017
↑ Terrano DT, Upreti M, Chambers TC. Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a functional link coupling mitotic arrest and apoptosis. Mol Cell Biol. 2010 Feb;30(3):640-56. doi: 10.1128/MCB.00882-09. Epub 2009 Nov, 16. PMID:19917720 doi:10.1128/MCB.00882-09
↑ Wang J, Beauchemin M, Bertrand R. Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints. Cell Signal. 2011 Dec;23(12):2030-8. doi: 10.1016/j.cellsig.2011.07.017. Epub, 2011 Aug 5. PMID:21840391 doi:10.1016/j.cellsig.2011.07.017
↑ Szigeti A, Bellyei S, Gasz B, Boronkai A, Hocsak E, Minik O, Bognar Z, Varbiro G, Sumegi B, Gallyas F Jr. Induction of necrotic cell death and mitochondrial permeabilization by heme binding protein 2/SOUL. FEBS Lett. 2006 Nov 27;580(27):6447-54. Epub 2006 Nov 7. PMID:17098234 doi:http://dx.doi.org/10.1016/j.febslet.2006.10.067
↑ Ambrosi E, Capaldi S, Bovi M, Saccomani G, Perduca M, Monaco HL. Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Biochem J. 2011 Jun 6. PMID:21639858 doi:10.1042/BJ20110257

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3r85"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human SOUL BH3 domain in complex with Bcl-xL==
-<StructureSection load='3r85' size='340' side='right' caption='[[3r85]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='3r85' size='340' side='right'caption='[[3r85]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3r85]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<table><tr><td colspan='2'>[[3r85]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r8j|3r8j]], [[3r8k|3r8k]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r8j|3r8j]], [[3r8k|3r8k]]</div></td></tr>
-<tr id='gene'><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 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCL2L1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3r85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r85 OCA], [http://pdbe.org/3r85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r85 RCSB], [http://www.ebi.ac.uk/pdbsum/3r85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r85 ProSAT]</span></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=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>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/HEBP2_HUMAN HEBP2_HUMAN]] Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.<ref>PMID:17098234</ref>
+[[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>  [[https://www.uniprot.org/uniprot/HEBP2_HUMAN HEBP2_HUMAN]] Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.<ref>PMID:17098234</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 3r85" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
 == References ==
 <references/>
@@ Line 25: / Line 28: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Ambrosi, E K]]
 [[Category: Bovi, M]]

3r85

From Proteopedia

Revision as of 05:52, 15 June 2022

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox