Fig. 8

Probable docking conformations of hEC1 with L. donovani Inl-A-like proteins. a L. monocytogenes Inl-A internalin domain crystal structure in complex with hEC1 [PDB ID: 1O6S]. b-d Representative best-docked conformation of L. donovani Inl-A-like proteins with hEC1 similar to Inl-A-hEC1 interaction for E9B7L9 (region: 212–573) (b), E9BMT7 (region: 394–757) (c), and E9BUL5 (region: 386–782) (d). Key interacting residues probably involved in forming hydrogen bond interactions or hydrophobic interactions in E9B7L9-hEC1, E9BMT7-hEC1 and E9BUL5-hEC1 complexes are also shown. Ranked solutions from each program having ligand RMSD (l-RMSD) with Inl-A crystal structure within 10 Å were compared and best poses as predicted by HADDOCK [52–54] are shown here as representatives. In cases where hydrogen bond forming residue overlaps with hydrophobic interaction forming residue precedence is given to hydrogen bond color code while the residue is shown in ball and stick conformation to indicate that it is probably involved in hydrophobic interaction as well