Figure 6
From: The α-helical regions of KERP1 are important in Entamoeba histolytica adherence to human cells
Three-dimensional structure prediction of KERP1 trimeric coiled-coil regions.
Three-dimensional modeling of the CC regions predicted for KERP1 according to COILS results. CC regions of KERP1 correspond to the KCS protein designated as, CC1 (Valine23 to Glutamine52), CC2 (Leucine55 to Lysine98) and CC3 (Lysine100 to Valine122), folded as elongated trimer. Modeling was performed using chain A of PDB file ID 1WT6 as template with its distinctive trimeric coiled-coil organization. Each of the three alpha helical ribbon chains is colored differently in order to differentiate them. Under the ribbons CPK model highlight the presence of positively charged residues (blue) and negatively charged residues (red). The most stable coiled coil trimer corresponds to CC3 (residues Lys-100 to Val-122) according to an electrostatic analysis on each of the CC predicted regions and the calculated values of free energy present for each, represented in the bottom of the CPK models.
