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Special Focus Review

STAT2

A shape-shifting anti-viral super STAT

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Article: e23633 | Published online: 01 Jan 2013

Figures & data

Table 1. STAT2 antagonism by viral proteins

Figure 1. Sequence similarity of STAT family members among select mammalian species. The full length protein sequences of STATs 1, 2, 3, 4, 5A and 6 were aligned against the human sequence for each of the species shown in the radar plot. The Clustal alignment algorithm within MacVector was used for the alignment, and the percent sequence similarity to human in pair-wise comparisons is plotted in the graph.

Figure 1. Sequence similarity of STAT family members among select mammalian species. The full length protein sequences of STATs 1, 2, 3, 4, 5A and 6 were aligned against the human sequence for each of the species shown in the radar plot. The Clustal alignment algorithm within MacVector was used for the alignment, and the percent sequence similarity to human in pair-wise comparisons is plotted in the graph.

Figure 2. Phylogenetic relationship between STAT1 and STAT2 among select mammals and non-human primates. The full length sequences of STAT1 and STAT2 for each species shown were aligned with the Clustal algorithm within MacVector. Phylogenetic analysis was performed with this alignment, and the scale indicates the absolute numbers of sequence differences across the length of the dendrogram.

Figure 2. Phylogenetic relationship between STAT1 and STAT2 among select mammals and non-human primates. The full length sequences of STAT1 and STAT2 for each species shown were aligned with the Clustal algorithm within MacVector. Phylogenetic analysis was performed with this alignment, and the scale indicates the absolute numbers of sequence differences across the length of the dendrogram.

Figure 3. The STAT2 C-terminus is highly divergent across species. The sequences of STAT2 from the indicated species were aligned beginning with residue 651 of human STAT2. The SH2 and C-terminus of STAT2 is indicated along with the conserved tyrosine residue (Y690), which is phosphorylated in responses to IFN-α/β signaling.

Figure 3. The STAT2 C-terminus is highly divergent across species. The sequences of STAT2 from the indicated species were aligned beginning with residue 651 of human STAT2. The SH2 and C-terminus of STAT2 is indicated along with the conserved tyrosine residue (Y690), which is phosphorylated in responses to IFN-α/β signaling.