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Fig. 1 | Malaria Journal

Fig. 1

From: Bioinformatic and literature assessment of toxicity and allergenicity of a CRISPR-Cas9 engineered gene drive to control Anopheles gambiae the mosquito vector of human malaria

Fig. 1

Sequence alignment between hCas9 and VapC. The domains within the hCas9 protein are illustrated in colour in the top box graphic [43], with all numbers corresponding to amino acids in hCas9, and regions of alignment to VapC (green box graphic) indicated by the dotted lines. From N- to C-terminus of hCas9, domains are “3 × FLAG” (coloured brown): FLAG epitopes in three tandem repeats positioned at the N-terminus of hCas9; “NLS” (purple): Nuclear localization signal; “RuvC-I” (red): RuvC domain I; “Arg” (silver): Arginine-rich domain; “Alpha-helical lobe” (orange); “RuvC-II” (red): RuvC domain II; “HNH” (blue): NHN nuclease domain; “RuvC-III” (red): RuvC domain III; “Topo” (dark grey): topo-homology domain; “CTD” (yellow): C-terminal domain [43]. Red triangles indicate catalytic residues in the RuvC-III domain [43]. Amino acid sequence alignments between hCas9 and VapC are shown below box graphics, with blue- and red- coloured amino acids from NHN and RuvC-III domains of hCas9, respectively, and VapC amino acids shown in green below [43]. Identical amino acids between both proteins are indicated by asterisks

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