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==Solution structure of the MLKL N-terminal domain==
==Solution structure of the MLKL N-terminal domain==
<StructureSection load='2msv' size='340' side='right'caption='[[2msv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2msv' size='340' side='right'caption='[[2msv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2msv]] is a 1 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=2MSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2msv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSV FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MLKL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msv OCA], [https://pdbe.org/2msv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msv RCSB], [https://www.ebi.ac.uk/pdbsum/2msv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msv 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=2msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msv OCA], [https://pdbe.org/2msv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msv RCSB], [https://www.ebi.ac.uk/pdbsum/2msv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MLKL_HUMAN MLKL_HUMAN]] Required for the execution of programmed necrosis.<ref>PMID:22265414</ref> 
[https://www.uniprot.org/uniprot/MLKL_HUMAN MLKL_HUMAN] Required for the execution of programmed necrosis.<ref>PMID:22265414</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MLKL is crucial for necroptosis, permeabilizing membranes through its N-terminal region upon phosphorylation of its kinase-like domain by RIP3. However, the mechanism underlying membrane permeabilization is unknown. The solution structure of the MLKL N-terminal region determined by nuclear magnetic resonance spectroscopy reveals a four-helix bundle with an additional helix at the top that is likely key for MLKL function, and a sixth, C-terminal helix that interacts with the top helix and with a poorly packed interface within the four-helix bundle. Fluorescence spectroscopy measurements indicate that much of the four-helix bundle inserts into membranes, but not the C-terminal helix. Moreover, we find that the four-helix bundle is sufficient to induce liposome leakage and that the C-terminal helix inhibits this activity. These results suggest that the four-helix bundle mediates membrane breakdown during necroptosis and that the sixth helix acts as a plug that prevents opening of the bundle and is released upon RIP3 phosphorylation.
 
A Plug Release Mechanism for Membrane Permeation by MLKL.,Su L, Quade B, Wang H, Sun L, Wang X, Rizo J Structure. 2014 Oct 7;22(10):1489-500. doi: 10.1016/j.str.2014.07.014. Epub 2014 , Sep 11. PMID:25220470<ref>PMID:25220470</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2msv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Quade, B]]
[[Category: Quade B]]
[[Category: Rizo, J]]
[[Category: Rizo J]]
[[Category: Su, L]]
[[Category: Su L]]
[[Category: Sun, L]]
[[Category: Sun L]]
[[Category: Wang, H]]
[[Category: Wang H]]
[[Category: Wang, X]]
[[Category: Wang X]]
[[Category: Membrane pore]]
[[Category: Membrane protein]]

Latest revision as of 10:02, 1 May 2024

Solution structure of the MLKL N-terminal domainSolution structure of the MLKL N-terminal domain

Structural highlights

2msv is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MLKL_HUMAN Required for the execution of programmed necrosis.[1]

References

  1. ↑ Wang Z, Jiang H, Chen S, Du F, Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell. 2012 Jan 20;148(1-2):228-43. doi: 10.1016/j.cell.2011.11.030. PMID:22265414 doi:http://dx.doi.org/10.1016/j.cell.2011.11.030
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