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. 2020 Oct 13;6:70. doi: 10.1038/s41421-020-00201-w

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a Homotetrameric packing of caspase-11 CARD in crystal. The H1–2 helices reside in the center of the interaction interfaces. b A stereo diagram of superimposed known CARD structures: CARMA1-CARD (PDB ID: 4jup), caspase-1-CARD (PDB ID: 5fna), RIP2-CARD (PDB ID: 6ggs), ASC-CARD (PDB ID: 5gpq), NLRC4-CARD (PDB ID: 6n1i), and caspase-11 CARD. c Sequence alignment of residues 1–101 of caspase-11, caspase-4, mcaspsae-1, hcaspase-1, ASC, and mNLRC4. Different amino acids are in white and conserved residues are highlighted in red. The secondary structure of caspase-11 CARD is shown above the sequence. d An electrostatic surface of Chain C generated with APBS software. Negatively charged regions are represented in red, neutral regions in white, and positively charged regions in blue. Locations of the hydrophobic interface are indicated. The N terminus sequence of H1–2 contains neutral amino acids (white). The direction of the chain (N–C terminus) is colored as blue to red. e An electrostatic surface representation of Chain A and D generated with APBS software. Negatively charged regions are represented in red, neutral regions in white, and positively charged regions in blue. Locations of the hydrophobic interface are indicated. For each chain, the N terminus sequence of H1–2 contains neutral amino acids (white). The direction of the chain (N–C terminus) is colored as blue to red.