Skip to main content
Fig. 6 | Parasites & Vectors

Fig. 6

From: Aminoacyl tRNA synthetases as potential drug targets of the Panthera pathogen Babesia

Fig. 6

Analysis of CLD binding site in KRSs from Babesia spp. and P. tigris. a Sequence alignment of KRSs. The two key residues are highlighted in a black box and other conserved residues responsible for CLD binding are shown in blue boxes. b Structural superimposition of Hs-KRS (PDB: 4YCU), Pf-KRS (PDB: 4PG3), P. tigris and three Babesia spp. (Bb, B. bovis; Bm, B. microti and Bg, B. bigemina) (built structure model, this study). The smaller CLD selectivity residues of cysteine-serine (for Bb, Bg) and valine-threonine (for Bm) may accommodate CLD in the binding pocket of Babesia KRSs. The bulkier glutamine-threonine (for Hs, H. sapiens; Pt, P. tigris) potentially hinder high potency CLD binding. Abbreviations: CLD, cladosporin; KRS, lysyl-tRNA synthetase

Back to article page