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4MWI

Crystal structure of the human MLKL pseudokinase domain

Summary for 4MWI
Entry DOI10.2210/pdb4mwi/pdb
Related4BTF
DescriptorMixed lineage kinase domain-like protein, (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol, GLYCEROL, ... (4 entities in total)
Functional Keywordspseudokinase, necroptosis, transferase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q8NB16
Total number of polymer chains1
Total formula weight34028.35
Authors
Czabotar, P.E.,Murphy, J.M. (deposition date: 2013-09-25, release date: 2013-12-04, Last modification date: 2023-09-20)
Primary citationMurphy, J.M.,Lucet, I.S.,Hildebrand, J.M.,Tanzer, M.C.,Young, S.N.,Sharma, P.,Lessene, G.,Alexander, W.S.,Babon, J.J.,Silke, J.,Czabotar, P.E.
Insights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKL.
Biochem.J., 457:369-377, 2014
Cited by
PubMed Abstract: The pseudokinase MLKL (mixed lineage kinase domain-like) was identified recently as an essential checkpoint in the programmed necrosis or 'necroptosis' cell death pathway. In the present study, we report the crystal structure of the human MLKL pseudokinase domain at 1.7 Å (1 Å=0.1 nm) 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, the present study provides insights into the evolution of nucleotide-binding mechanisms among pseudokinases and their mechanistic divergence from conventional catalytically active protein kinases.
PubMed: 24219132
DOI: 10.1042/BJ20131270
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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