Figure 1
From: The α-helical regions of KERP1 are important in Entamoeba histolytica adherence to human cells
KERP1 protein domains predicted by bioinformatics analysis.
(a). Analysis of KERP1 primary structure using the COILS and Pfam servers. The coiled-coil domain (KCS) is highlighted in grey (from amino acid 23 to 122) and the Universal Stress Protein (Usp) domain (amino acid 26 to 103) is underlined in black. (b). Graphical representation of the COILS server prediction output using the complete amino acid sequence of KERP1 (Accession number EHI_098210). (c). Coiled-coil domain segments of KERP1 CC1 (residues 23 to 52), CC2 (residues 55 to 98) and CC3 (residues 101 to 122) are represented using the heptad repeat (a-b-c-d-e-f-g)n assignation from COILS prediction.
