4MWI
Crystal structure of the human MLKL pseudokinase domain
Summary for 4MWI
| Entry DOI | 10.2210/pdb4mwi/pdb |
| Related | 4BTF |
| Descriptor | Mixed 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 Keywords | pseudokinase, necroptosis, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q8NB16 |
| Total number of polymer chains | 1 |
| Total formula weight | 34028.35 |
| Authors | Czabotar, P.E.,Murphy, J.M. (deposition date: 2013-09-25, release date: 2013-12-04, Last modification date: 2023-09-20) |
| Primary citation | Murphy, 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: 24219132DOI: 10.1042/BJ20131270 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
