4m68
From Proteopedia
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- | {{STRUCTURE_4m68| PDB=4m68 | SCENE= }} | ||
- | ===Crystal structure of the mouse MLKL kinase-like domain=== | ||
- | == | + | ==Crystal structure of the mouse MLKL kinase-like domain== |
- | [[http://www.uniprot.org/uniprot/MLKL_MOUSE MLKL_MOUSE | + | <StructureSection load='4m68' size='340' side='right'caption='[[4m68]], [[Resolution|resolution]] 1.70Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4m68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M68 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.696Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4m68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m68 OCA], [https://pdbe.org/4m68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m68 RCSB], [https://www.ebi.ac.uk/pdbsum/4m68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m68 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MLKL_MOUSE MLKL_MOUSE] Required for the execution of programmed necrosis (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | RIP3 is an essential upstream kinase in necroptosis. The pseudokinase MLKL functions as a substrate of RIP3 to mediate downstream signaling. The molecular mechanism by which RIP3 recognizes and phosphorylates MLKL remains unknown. Here, we report the crystal structures of the mouse RIP3 kinase domain, the MLKL kinase-like domain, and a binary complex between the two. Both RIP3 and MLKL adopt the canonical kinase fold. Free RIP3 exists in an active conformation, whereas MLKL-bound RIP3 is stabilized by AMP-PNP to adopt an inactive conformation. The formation of the RIP3-MLKL complex, involving their respective N- and C-lobes, is accompanied by pronounced conformational changes of the alphaC helix and activation loop in RIP3 and the corresponding structural elements in MLKL. RIP3-mediated MLKL phosphorylation, though important for downstream signaling, is dispensable for stable complex formation between RIP3 and MLKL. Our study serves as a framework for mechanistic understanding of RIP3-mediated necroptotic signaling. | ||
- | + | Structural Insights into RIP3-Mediated Necroptotic Signaling.,Xie T, Peng W, Yan C, Wu J, Gong X, Shi Y Cell Rep. 2013 Oct 17;5(1):70-8. doi: 10.1016/j.celrep.2013.08.044. Epub 2013 Oct, 3. PMID:24095729<ref>PMID:24095729</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4m68" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Peng | + | [[Category: Peng W]] |
- | [[Category: Shi | + | [[Category: Shi Y]] |
- | [[Category: Wu | + | [[Category: Wu J]] |
- | [[Category: Xie | + | [[Category: Xie T]] |
- | [[Category: Yan | + | [[Category: Yan C]] |
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Current revision
Crystal structure of the mouse MLKL kinase-like domain
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Categories: Large Structures | Mus musculus | Peng W | Shi Y | Wu J | Xie T | Yan C