Conservation among species
The multiple sequence alignment (MSA) that was generated scored particularly well in two delimited regions: one matching the sequence segment identified to be part of the interface between chain L and chain N, and the other matched the interface between chain L and I.
Four residues appear to be conserved in the interface between chains L and N, namely: TYR191, ILE192, TYR193, and ASN194
The interface between L and I appears to have 7 conserved residues: LYS104, ALA105, VAL109, ILE110, MET111, PRO113, and ILE114
Generally, hydrophilic residues seem to be more frequently conserved, perhaps due to their involvement in forming high-energy bonds
MSA of several IML3 homologous proteins. The residues in the binding interface with CHL4 are enclosed in black borders, with highly conserved residues indicated by arrows.
MSA of several IML3 homologous proteins. The residues in the binding interface with CTF3 are enclosed in black borders, with highly conserved residues indicated by arrows.