CCR3, a G protein-coupled receptor, plays a central role in allergic 
inflammation and is an important drug target for inflammatory diseases. To 
understand the structure-function relationship of CCR3 receptor, different 
computational techniques were employed, which mainly include: (i) homology 
modeling of CCR3 receptor, (ii) 3D-quantitative pharmacophore model of CCR3 
antagonists, (iii) virtual screening of small compound databases, and (iv) 
finally, molecular docking at the binding site of the CCR3 receptor homology 
model. Pharmacophore model was developed for the first time, on a training data 
set of 22 CCR3 antagonists, using CATALYST HypoRefine program. Best hypothesis 
(Hypo1) has three different chemical features: two hydrogen-bond acceptors, one 
hydrophobic, and one ring aromatic. Hypo1 model was further validated using (i) 
87 test set CCR3 antagonists, (ii) Cat Scramble randomization technique, and 
(iii) Decoy data set. Molecular docking studies were performed on modeled CCR3 
receptor using 303 virtually screened hits, obtained from small compound 
database virtual screening. Finally, five hits were identified as potential 
leads against CCR3 receptor, which exhibited good estimated activities, 
favorable binding interactions, and high docking scores. These studies provided 
useful information on the structurally vital residues of CCR3 receptor involved 
in the antagonist binding, and their unexplored potential for the future 
development of potent CCR3 receptor antagonists.