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2msv
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2msv]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSV FirstGlance]. <br> | <table><tr><td colspan='2'>[[2msv]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MSV FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2msv RCSB], [http://www.ebi.ac.uk/pdbsum/2msv PDBsum]</span></td></tr> | + | </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=2msv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2msv RCSB], [http://www.ebi.ac.uk/pdbsum/2msv PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:55, 29 October 2014
Solution structure of the MLKL N-terminal domain
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Categories: Quade, B. | Rizo, J. | Su, L. | Sun, L. | Wang, H. | Wang, X. | Membrane pore | Membrane protein
