A directed docking was performed using Cluspro between human PDGF-BB and EGFR using specific templates obtained from PDB. Various conserved residues were found to be involved in the docking interaction of the complex by means of hydrophobic interactions and hydrogen bonds. An electrostatic potential evaluation of the PDGF-BB-EGFR complex was also performed to validate if the complex is electrostatically complementary in the binding area. Results suggested a possible binding mechanism which could explain the in vivo evidence of formation of heterodimeric receptors EGFR-PDGFR. © Springer International Publishing Switzerland 2014.