6x8o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==BimBH3 peptide tetramer==
==BimBH3 peptide tetramer==
-
<StructureSection load='6x8o' size='340' side='right'caption='[[6x8o]]' scene=''>
+
<StructureSection load='6x8o' size='340' side='right'caption='[[6x8o]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X8O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X8O FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6x8o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X8O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X8O FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x8o OCA], [http://pdbe.org/6x8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x8o RCSB], [http://www.ebi.ac.uk/pdbsum/6x8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x8o ProSAT]</span></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
 +
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x8o OCA], [http://pdbe.org/6x8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x8o RCSB], [http://www.ebi.ac.uk/pdbsum/6x8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x8o ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/B2L11_HUMAN B2L11_HUMAN]] Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis.<ref>PMID:9430630</ref> <ref>PMID:11734221</ref> <ref>PMID:12019181</ref> <ref>PMID:11997495</ref> <ref>PMID:15147734</ref> <ref>PMID:15486195</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Bcl-2 proteins orchestrate the mitochondrial pathway of apoptosis, pivotal for cell death. Yet, the structural details of the conformational changes of pro- and antiapoptotic proteins and their interactions remain unclear. Pulse dipolar spectroscopy (double electron-electron resonance [DEER], also known as PELDOR) in combination with spin-labeled apoptotic Bcl-2 proteins unveils conformational changes and interactions of each protein player via detection of intra- and inter-protein distances. Here, we present the synthesis and characterization of pro-apoptotic BimBH3 peptides of different lengths carrying cysteines for labeling with nitroxide or gadolinium spin probes. We show by DEER that the length of the peptides modulates their homo-interactions in the absence of other Bcl-2 proteins and solve by X-ray crystallography the structure of a BimBH3 tetramer, revealing the molecular details of the inter-peptide interactions. Finally, we prove that using orthogonal labels and three-channel DEER we can disentangle the Bim-Bim, Bcl-xL-Bcl-xL, and Bim-Bcl-xL interactions in a simplified interactome.
 +
 +
Biophysical Characterization of Pro-apoptotic BimBH3 Peptides Reveals an Unexpected Capacity for Self-Association.,Assafa TE, Nandi S, Smilowicz D, Galazzo L, Teucher M, Elsner C, Putz S, Bleicken S, Robin AY, Westphal D, Uson I, Stoll R, Czabotar PE, Metzler-Nolte N, Bordignon E Structure. 2020 Sep 14. pii: S0969-2126(20)30327-0. doi:, 10.1016/j.str.2020.09.002. PMID:32966763<ref>PMID:32966763</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6x8o" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Czabotar PE]]
+
[[Category: Czabotar, P E]]
-
[[Category: Robin AY]]
+
[[Category: Robin, A Y]]
-
[[Category: Uson I]]
+
[[Category: Uson, I]]
-
[[Category: Westphal D]]
+
[[Category: Westphal, D]]
 +
[[Category: Apoptosis]]
 +
[[Category: Bcl-2]]
 +
[[Category: Bh3]]
 +
[[Category: Bim]]
 +
[[Category: Cell death]]

Revision as of 06:40, 7 October 2020

BimBH3 peptide tetramer

PDB ID 6x8o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools