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Fig. 3 | Malaria Journal

Fig. 3

From: Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparum

Fig. 3

a Cartoon representation of homology models of cold shock protein domain of PfCoSP (28–73 amino acids) and its homologues in Plasmodium vivax (PVBG_03557, 34–102 amino acid residues) and Plasmodium berghei (PBANKA_020400; 36–85 amino acid residues). Five beta chains forming the oligonucleotide binding-fold are labelled. b Multiple sequence alignment of human YBOX-1 with PfCoSP and its homologues in other Plasmodium species. Residues known to form RNA binding site and those involved in dimerization in YBOX-1 and their corresponding residues in other cold shock protein members are marked with green and yellow bars, respectively. c Surface representation of human YB-1 and cold shock protein domain of PfCoSP, and its homologues in Plasmodium vivax (PVBG_03557) and Plasmodium berghei (PBANKA_020400). Residues responsible for human YB-1 dimerization and their corresponding residues in PfCoSP, P. vivax (PVBG_03557) and P. berghei (PBANKA_020400) cold shock proteins are shown in red, and are labelled. Y99 and V68 of human YB-1 and their corresponding residues that are not conserved in PfCoSP, P. vivax (PVBG_03557) and P. berghei (PBANKA_020400) are labelled in black and yellow, respectively. K78 of P. vivax cold shock protein (PVBG_03557) and V70 of P. berghei (PBANKA_020400) are obscured from view in the depicted orientation

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