Fig. 3From: Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparuma 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 orientationBack to article page