4MWI

Crystal structure of the human MLKL pseudokinase domain

4MWI の概要

• エントリーDOI: 10.2210/pdb4mwi/pdb
• 関連するPDBエントリー: 4BTF
• 分子名称: 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)
• 機能のキーワード: pseudokinase, necroptosis, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q8NB16
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34028.35

構造登録者

Czabotar, P.E.,Murphy, J.M. (登録日: 2013-09-25, 公開日: 2013-12-04, 最終更新日: 2023-09-20)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.7 Å)