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Figure 3 | Virology Journal

Figure 3

From: An ectromelia virus profilin homolog interacts with cellular tropomyosin and viral A-type inclusion protein

Figure 3

Structural comparison of the poly(L-proline) binding site of ECTV-PH and human profilin 1. (A) Surface diagrams of the ECTV-PH structural model and the human profilin 1 crystal structure using a blue background with the important poly(L-proline) binding residues coloured in green. The dark red residue represents the one residue (W-5 in ECTV-PH, W-3 in human profilin 1) that is identical between both structures; the orange residue represents the one functionally conserved residue (V-129 in ECTV-PH, L-134 in human profilin 1). (B) Surface diagrams of ECTV-PH and human profilin 1 with residues coloured by amino acid property as follows: aromatic residues (F, Y, W) in purple; negatively charged residues (D, E) in red; positively charged residues (R, H, K) in dark blue; non-polar/aliphatic residues (G, I, L, M, V) in gold; and polar/uncharged residues (N, Q, P, S, T) in light blue.

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