2msv

Solution structure of the MLKL N-terminal domain

spinqualitylabelsall models 2msv, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2msv is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Function [MLKL_HUMAN] Required for the execution of programmed necrosis. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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