Fig. 2 | Nature Communications

Fig. 2

From: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses

Fig. 2

Structural comparisons and basis for high affinity interaction of HeV W with importin α3. Importin α1:HeV W and importin α3:HeV W structures were solved to 2.2 Å and 1.6 Å resolution, respectively. The importin α adaptors are shown in cartoon and surface representation (importin α1: bright yellow, importin α3: light orange) and HeV W NLS in stick representation (magenta: carbon atoms, red: oxygen atoms, blue: nitrogen atoms) with associated simulated annealing Fo-Fc omit maps of the NLSs contoured to 3σ in green. Schematics of the binding interface and specific interactions are shown below (magenta: carbon atoms, red: oxygen atoms, blue: nitrogen atoms), with hydrogen bond and salt bridge interactions depicted by dash lines (black and red respectively), and the partner interactions for importin α1 (bold italics) and importin α3 coloured as orange: carbon atoms, red: oxygen atoms, blue: nitrogen atoms. The location of these interactions in the ARM repeats highlight the greater interaction interface of the HeV W NLS for the importin α3 adaptor

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