The leukotriene B₄ receptors BLT₁ and BLT₂ are promising targets for the treatment of allergic and inflammatory diseases. However, no working model of ligand binding to either of these receptors has been developed so far. Under the assumption that homologous receptors bind their ligands in a similar way, computational modeling of agonist binding to BLT₁ and BLT₂ was performed using fully flexible docking in Galaxy 7TM. For both receptors, the carboxyl group of the ligand forms a salt bridge with an arginine residue, while the tail hydroxyl groups form hydrogen bonds with three amino acid residues. The differential specificity of ligands to BLT₁ and BLT₂ is explained by the replacement of histidine with tyrosine. In BLT₁, the histidine residue binds the 5-OH group of the ligand, while the tyrosine residue in BLT₂ repels it. The presented models are in agreement with experimental data and may be useful for developing new BLT₁- and BLT₂-targeted drugs.