4mwi: Difference between revisions

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'''Unreleased structure'''


The entry 4mwi is ON HOLD
==Crystal structure of the human MLKL pseudokinase domain==
<StructureSection load='4mwi' size='340' side='right'caption='[[4mwi]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mwi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MWI 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]] 1.7&#8491;</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>, <scene name='pdbligand=PXN:(2S)-1-[3-{[(2R)-2-HYDROXYPROPYL]OXY}-2,2-BIS({[(2R)-2-HYDROXYPROPYL]OXY}METHYL)PROPOXY]PROPAN-2-OL'>PXN</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=4mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mwi OCA], [https://pdbe.org/4mwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mwi RCSB], [https://www.ebi.ac.uk/pdbsum/4mwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mwi ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
The pseudokinase, Mixed lineage kinase domain-like (MLKL), was recently identified as an essential checkpoint in the programmed necrosis or "necroptosis" cell death pathway. Here, we present the crystal structure of the human MLKL pseudokinase domain at 1.7 A resolution and probe its nucleotide-binding mechanism by performing structure-based mutagenesis. By comparing the structures and nucleotide binding determinants of human and mouse MLKL orthologues, our study provides insights into the evolution of nucleotide binding mechanisms amongst pseudokinases and their mechanistic divergence from conventional, catalytically-active protein kinases.


Authors: Czabotar, P.E., Murphy, J.M.
Insights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKL.,Murphy JM, Lucet IS, Hildebrand JM, Tanzer MC, Young SN, Sharma P, Lessene G, Alexander WS, Babon JJ, Silke J, Czabotar PE Biochem J. 2013 Nov 13. PMID:24219132<ref>PMID:24219132</ref>


Description: Crystal structure of the human MLKL pseudokinase domain
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mwi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Czabotar PE]]
[[Category: Murphy JM]]

Latest revision as of 16:44, 20 September 2023

Crystal structure of the human MLKL pseudokinase domain

4mwi, resolution 1.70Å

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