6l8v
From Proteopedia
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==membrane-bound Bax helix2-helix5 domain== | ==membrane-bound Bax helix2-helix5 domain== | ||
| - | <StructureSection load='6l8v' size='340' side='right'caption='[[6l8v]]' scene=''> | + | <StructureSection load='6l8v' size='340' side='right'caption='[[6l8v]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[6l8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L8V FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAX, BCL2L4 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=6l8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8v OCA], [https://pdbe.org/6l8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l8v RCSB], [https://www.ebi.ac.uk/pdbsum/6l8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/BAX_HUMAN BAX_HUMAN]] Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.<ref>PMID:8358790</ref> <ref>PMID:10772918</ref> <ref>PMID:8521816</ref> <ref>PMID:16113678</ref> <ref>PMID:18948948</ref> <ref>PMID:21199865</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bax proteins form pores in the mitochondrial outer membrane to initiate apoptosis. This might involve their embedding in the cytosolic leaflet of the lipid bilayer, thus generating tension to induce a lipid pore with radially arranged lipids forming the wall. Alternatively, Bax proteins might comprise part of the pore wall. However, there is no unambiguous structural evidence for either hypothesis. Using NMR, we determined a high-resolution structure of the Bax core region, revealing a dimer with the nonpolar surface covering the lipid bilayer edge and the polar surface exposed to water. The dimer tilts from the bilayer normal, not only maximizing nonpolar interactions with lipid tails but also creating polar interactions between charged residues and lipid heads. Structure-guided mutations demonstrate the importance of both types of protein-lipid interactions in Bax pore assembly and core dimer configuration. Therefore, the Bax core dimer forms part of the proteolipid pore wall to permeabilize mitochondria. | ||
| + | |||
| + | An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial membrane.,Lv F, Qi F, Zhang Z, Wen M, Kale J, Piai A, Du L, Wang S, Zhou L, Yang Y, Wu B, Liu Z, Del Rosario J, Pogmore J, Chou JJ, Andrews DW, Lin J, OuYang B EMBO J. 2021 Jul 15;40(14):e106438. doi: 10.15252/embj.2020106438. Epub 2021 Jun , 8. PMID:34101209<ref>PMID:34101209</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6l8v" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Lv, F]] |
| - | [[Category: | + | [[Category: OuYang, B]] |
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Bax]] | ||
| + | [[Category: Core-domain]] | ||
| + | [[Category: Dimer]] | ||
| + | [[Category: Membrane-bound]] | ||
| + | [[Category: Stability]] | ||
Revision as of 12:40, 24 November 2021
membrane-bound Bax helix2-helix5 domain
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Categories: Human | Large Structures | Lv, F | OuYang, B | Apoptosis | Bax | Core-domain | Dimer | Membrane-bound | Stability
