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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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Image Search Results


a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.

Journal: bioRxiv

Article Title: Structure of zebrafish NLRP3 reveals a novel mode of inflammasome activation

doi: 10.64898/2026.04.17.719140

Figure Lengend Snippet: a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.

Article Snippet: Human full-length ASC was cloned into pLenti-EF1a-C-tGFP (Origene, PS100072) and tGFP was exchanged with YFP.

Techniques: Sequencing, SDS Page