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. Author manuscript; available in PMC: 2015 Apr 20.
Published in final edited form as: Biochim Biophys Acta. 2013 Sep 30;1838(1 0 0):185–192. doi: 10.1016/j.bbamem.2013.09.014

Fig. 1.

Fig. 1

Association of malaria proteins with ankyrin R. (A) Binding of ankyrin R to KAHRP fragments. Schematic representation of KAHRP (a). The binding between ankyrin R and KAHRP fragments was assessed by pull-down (b) and ELISA assay (c). Note that ankyrin R bound to only the K1D fragment of the KAHRP. (B) Binding of ankyrin R to PfEMP3 fragments. Schematic representation of PfEMP3 (a). The binding between ankyrin R and PfEMP3 fragments was assessed by pull-down (b). Repeats 14–15 fragment of β-spectrin was used as a positive control for ankyrin R binding. (C) Binding of ankyrin R to RESA fragments. Schematic representation of RESA (a). The binding between ankyrin R and RESA fragments was assessed by pull-down (b). Repeats 14–15 fragment of β-spectrin was used as a positive control for ankyrin R binding. (D) Binding of ankyrin R to the cytoplasmic domain of PfEMP1. Schematic representation of PfEMP1 (a). The binding between ankyrin R and cytoplasmic domain of PfEMP1 was assessed by pull-down (b). Repeats 14–15 fragment of β-spectrin was used as a positive control for ankyrin R binding. Amino acid residue numbers and the lengths of fragments are indicated.