Structure-based sequence alignment of <i>rhes</i>IE1, <i>hum</i>IE1 and <i>rat</i>IE1.

Abstract

Structure-based sequence alignment calculated with PROMALS3D [32]. The sequences of rhesIE1, humIE1 and ratIE1 were aligned according to the experimental structures. Helix designations were taken from rhesIE1 structure (PDB: 4WID:B). Residues identical in all three structures are marked by an asterisk (*). The handedness of coiled-coils in the structures of rhesIE1, humIE1 and ratIE1 is marked in yellow (left-handed) or cyan (right-handed). The hydrophilic residues of the three-residue insertions are marked in magenta. Residues occupying the a, d or h positions of heptad or hendecad repeats are shown in boldface. Regions without possible repeats are printed in lower case. The sequence of murIE1 was manually fitted to the aligned sequences. Putative residues involved in heptad or hendecad repeats are indicated as described above. (TIF)</p