Figure 7.
Variants in positively charged patches flanking the binding valley of SLFN14 result in altered protein function. (A) Sequence homology between human SLFN14 and SLFN13 shows conservation of positively charged amino acid side chains for known TP-related variants (yellow highlight). “∗” indicates a fully conserved residue; “:” a conservation between groups of strongly similar properties, scoring >0.5 in the Gonnet PAM 250 matrix; and “.” a conservation between groups of weakly similar properties, scoring ≤0.5 in the Gonnet PAM 250 matrix. (B) Overview of the complete SLFN14 monomer (P0C7P3). Model based on known SLFN13 protein structure. Important function regions have been highlighted. (C) Closeup view of the valley region of SLFN14, containing positively charged residues with known variants related to TP (K218, K219, V220, and R223).

Variants in positively charged patches flanking the binding valley of SLFN14 result in altered protein function. (A) Sequence homology between human SLFN14 and SLFN13 shows conservation of positively charged amino acid side chains for known TP-related variants (yellow highlight). “∗” indicates a fully conserved residue; “:” a conservation between groups of strongly similar properties, scoring >0.5 in the Gonnet PAM 250 matrix; and “.” a conservation between groups of weakly similar properties, scoring ≤0.5 in the Gonnet PAM 250 matrix. (B) Overview of the complete SLFN14 monomer (P0C7P3). Model based on known SLFN13 protein structure. Important function regions have been highlighted. (C) Closeup view of the valley region of SLFN14, containing positively charged residues with known variants related to TP (K218, K219, V220, and R223).

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