7m5c: Difference between revisions
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==== | ==Crystal Structure of human BAK in complex with WT BAK BH3 peptide== | ||
<StructureSection load='7m5c' size='340' side='right'caption='[[7m5c]]' scene=''> | <StructureSection load='7m5c' size='340' side='right'caption='[[7m5c]], [[Resolution|resolution]] 3.06Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7m5c]] is a 20 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=7M5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M5C FirstGlance]. <br> | ||
</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=7m5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5c OCA], [https://pdbe.org/7m5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5c RCSB], [https://www.ebi.ac.uk/pdbsum/7m5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5c 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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7m5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5c OCA], [https://pdbe.org/7m5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5c RCSB], [https://www.ebi.ac.uk/pdbsum/7m5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/BAK_HUMAN BAK_HUMAN]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.<ref>PMID:8521816</ref> <ref>PMID:17157251</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BCL-2 proteins regulate mitochondrial poration in apoptosis initiation. How the pore-forming BCL-2 Effector BAK is activated remains incompletely understood mechanistically. Here we investigate autoactivation and direct activation by BH3-only proteins, which cooperate to lower BAK threshold in membrane poration and apoptosis initiation. We define in trans BAK autoactivation as the asymmetric "BH3-in-groove" triggering of dormant BAK by active BAK. BAK autoactivation is mechanistically similar to direct activation. The structure of autoactivated BAK BH3-BAK complex reveals the conformational changes leading to helix alpha1 destabilization, which is a hallmark of BAK activation. Helix alpha1 is destabilized and restabilized in structures of BAK engaged by rationally designed, high-affinity activating and inactivating BID-like BH3 ligands, respectively. Altogether our data support the long-standing hit-and-run mechanism of BAK activation by transient binding of BH3-only proteins, demonstrating that BH3-induced structural changes are more important in BAK activation than BH3 ligand affinity. | |||
Structural basis of BAK activation in mitochondrial apoptosis initiation.,Singh G, Guibao CD, Seetharaman J, Aggarwal A, Grace CR, McNamara DE, Vaithiyalingam S, Waddell MB, Moldoveanu T Nat Commun. 2022 Jan 11;13(1):250. doi: 10.1038/s41467-021-27851-y. PMID:35017502<ref>PMID:35017502</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7m5c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aggarwal A]] | ||
[[Category: Moldoveanu T]] | |||
[[Category: Singh G]] | |||
Revision as of 03:48, 8 September 2022
Crystal Structure of human BAK in complex with WT BAK BH3 peptide
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