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Fig. 1 | Chinese Journal of Cancer

Fig. 1

From: Structural analysis of tumor-related single amino acid mutations in human MxA protein

Fig. 1

Amino acid sequence alignment of myxovirus resistance (Mx) proteins and dynamins. Amino acid sequences of Mx proteins and dynamins from human, mouse, chicken, zebra fish, fruit fly, C. elegans, and yeast are shown in the sequence alignment (see the “Methods” for details). Residues with a conservation of greater than 70% are color-coded (negatively charged amino acid residues D and E in red; positively charged R, K, and H in blue; polar N, Q, S, and T in grey; weak or nonpolar A, L, I, V, F, Y, W, M, and C in green; and special P and G in brown). Numbers in square brackets in front of each 10-residue sequence fragment indicate the ordinal position of the first residue of this fragment at the primary structure of the corresponding protein. Tumor-associated mutations are indicated at the corresponding positions. Residues highly conserved in Mx proteins and dynamins (L95, P96, P218, V263, L619, E632, and L643) are shown in violet, residues showing considerable overall conservation (S134, R310, G392, and Y538) in magenta, residues conserved in Mx proteins but not in dynamins (K326, V449, S572, R649, and R654) in yellow, and residues with no conservativeness (T27, N491, R522, G540, T651, and R655) in cyan

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