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Literature summary for 3.4.22.64 extracted from

  • Liu, M.; Zhou, K.; Xu, Z.; Ma, H.; Cao, X.; Yin, X.; Zeng, W.; Zahid, A.; Fu, S.; Ni, K.; Ye, X.; Zhou, Y.; Bai, L.; Zhou, R.; Jin, T.
    Crystal structure of caspase-11 CARD provides insights into caspase-11 activation (2020), Cell Discov., 6, 70.
    View publication on PubMed
Search for more literature for 3.4.22.64

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of isolated wild-type and mutant N-terminally MBP-tagged and C-terminally His6-tagged caspase-11 CARD domains in Escherichia coli strains Rosetta and BL21(DE3), recombinant expression of C-terminally EGFP-tagged wild-type and mutant enzymes in HEK-293T cells Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant caspase-11 CARD, hanging drop vapor diffusion method, the well solution contains 2.4 M ammonium sulfate and 5% isopropanol, 18 C, 1 week, X-ray diffraction structure determination and analysis at 2.8 A resolution Mus musculus

Protein Variants

Protein Variants Comment Organism
C254A/K19E site-directed mutagenesis, mutations on the helix H1 2 located in the N-terminal side of CARD domain Mus musculus
K19E site-directed mutagenesis, the charge mutation positions in the middle of helix H1 2 Mus musculus
additional information mutations of the helix H1-2 hydrophobic residues abolish the tetramerization of MBP-tagged CARD in solution and fail to induce pyroptosis in cells. The mutations abolish the aggregation of caspase-11 CARD and prohibit the self-cleavage of caspase-11 Mus musculus
V13A/L14A/L17A/V21A site-directed mutagenesis, VLLV-caspase-11 mutant, mutations on the helix H1 2 located in the N-terminal side of CARD domain destroy the hydrophobic interactions Mus musculus
V28E site-directed mutagenesis, V28E-CARD mutant Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
gasdermin D + H2O Mus musculus
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P70343 cf. caspase-4, EC 3.4.22.57
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification tetrameric aggregation of caspase-11 is thought to promote the autoprocessing and activation of caspase-11, activation mechanism of caspase-11, overview. The tetramerization of the N-terminal CARD prevents catalytic domain autoinhibition, leading to the caspase-11 activation. The hydrophobic interface is critical for the cellular activation of the caspase-11 inflammasome Mus musculus

Purification (Commentary)

Purification (Comment) Organism
recombinant MBP-tagged caspase-11 CARD domain, recombinant EGFP-tagged wild-type and mutant enzymes from HEK-293T cells by affinity chromatography and gel filtration Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DABYL-GQLSLLSDGID-Glu + H2O synthetic substrate Mus musculus ?
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 ?
gasdermin D + H2O
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 Mus musculus ?
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 ?

Subunits

Subunits Comment Organism
additional information caspase-11 contains two components, an N-terminal caspase recruitment domain (CARD) and a C-terminal catalytic domain. The MBP-tagged caspase-11 CARD domain tetramerizes in solution. An extensive hydrophobic interface formed by the H1-2 helix mediates homotypic CARD interactions. The CARD mediates caspase oligomerization through CARD CARD interaction. The CARD of caspase-11 is essential for LPS-induced pyroptosis. Overall crystal structure of the caspase-11 CARD, overview Mus musculus

General Information

General Information Comment Organism
evolution caspase-11, -4, and -5 belong to a family of aspartate-specific cysteine proteases. Their activation requires oligomerization and autoproteolysis. Caspase-11, -4, and -5 contain an N-terminal death fold named caspase recruitment domain (CARD) and a C-terminal catalytic domain Mus musculus
malfunction mutations in the hydrophobic interface abolish the aggregation of caspase-11 in vitro Mus musculus
metabolism murine caspase-11 is the key enzyme of the non-canonical inflammasome pathway that can respond to intracellular LPS and induce pyroptosis. The hydrophobic interface is critical for the cellular activation of the caspase-11 inflammasome Mus musculus
additional information caspase-11-mediated gasdermin D (GSDMD) cleavage and cell death are dependent on the hydrophobic surface on H1 2 of CARD. The hydrophobic interface is critical for the cellular activation of the caspase-11 inflammasome Mus musculus
physiological function sensing of cytoplasmic lipopolysaccharide (LPS) results in the self-cleavage and activation of caspase-11. The activated caspase can then drive the canonical inflammasome pathway to induce pyroptosis. The activation of caspase-11 is involved in the development of inflammatory responses, such as lethal sepsis, making it an important target for drug development Mus musculus