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. 2013 Feb 18;9(2):e1003222. doi: 10.1371/journal.pgen.1003222

Figure 5. Three risk variants of IFIH1 and the proposed functional model.

Figure 5

(A) IFIH1 protein (1025 amino acids (aa)) structure shows four conserved domains (start-stop aa) in boxes: a caspase recruitment (CARD) domain 115–200 aa); a helicase ATP-binding domain (305–493 aa), a helicase C-terminal domain (743–826 aa), and a RIG-I regulatory domain (901–1022 aa). (B) Domain prediction by Pfam: Gene intron/exon structure is presented below, with exons represented by thick vertical lines. (C) The three associated SNPs are represented by arrowed boxes. SNP rs10930046 is located in the helicase ATP-binding domain encoded by exons 4–7; rs1990760 is located in the RIG-1 regulatory domain encoded by exons 14–16; rs13023380 is on intron 3. We present a model of the functions implicated by the risk alleles in each variant, where each identified variant has an effect on the expression of NFκ-B1, CASP9, MAVS, MX1, IFIT1, NFκ-B2, TNFA and MAPK8, and their impact on inflammation, viral response and transcription.