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. 2020 Oct 26;11:5405. doi: 10.1038/s41467-020-19259-x

Fig. 3. Details of the BBRF2Δ-BSRF1Δ interface.

Fig. 3

a Schematic showing the discernible residues of BBRF2Δ and BSRF1Δ in the BBRF2Δ-BSRF1Δ crystal complex (coloured region) compared to full-length BBRF2 and BSRF1. Colour as in Fig. 3b. b Two views of the constitutive heterodimer. Colour as in a. The N- and C-termini of BSRF1Δ are specified. c Hydrophobic interactions between the two antiparallel ɑ-helices of BSRF1Δ. d–f Detailed residue contact at the BBRF2Δ-BSRF1Δ interface. The hydrophobic interface (d), polar interface (e), and BSRF1 ΔN-terminal loop mediated interface (f) are shown. Secondary structural elements are labelled. Involved residues are coloured as the molecule to which they belong. g Surface conservation plot of BBRF2Δ (left) and BSRF1Δ (right). Associated BSRF1Δ (left) and BBRF2Δ (right) are shown with transparency for clarity. The interface of the BBRF2Δ-BSRF1Δ heterodimer is outlined in yellow.