Fig. 1: POLE exonuclease domain variants studied in this work. | Genetics in Medicine

Fig. 1: POLE exonuclease domain variants studied in this work.

From: Genetic, structural, and functional characterization of POLE polymerase proofreading variants allows cancer risk prediction

Fig. 1

(a) Surface representation of the exonuclease domain (residues 268–471). (Inset) Mutated residues are highlighted to demonstrate clustering of the variants in and around the DNA binding pocket. (b) Schematic representation of human POLE gene showing the exonuclease (Exo) and polymerase domains. Exons are shown as multicolored boxes. (c) Sequence alignment demonstrating that the eight residues (P286, M294, P324, N363, D368, L424, K425, P436) studied in this work are invariant in POLE orthologs. The missense variants are indicated by closed arrows. Conserved Exo motifs I–V are highlighted in pink and the four conserved acidic metal-binding residues are indicated by an asterisk.

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