Waraphan TonitiPranom PuchadapiromAekkapot ChamkasemTawewan TansatitMahidol University. Faculty of Veterinary Science. Department of Pre-clinic and Applied Animal SciencesMahidol University. Faculty of Science. Department of Pathobiology2018-06-062018-06-062018-062012Journal of Applied Animal Science. Vol.5, No.2 (2012), 35-421906-2257https://repository.li.mahidol.ac.th/handle/20.500.14594/13319Beta 2-adrenergic Receptors are widely distributed in heart, airway smooth muscle, liver, skeletal muscle and adipose tissue. The specific ligand, beta 2-agonist, binds at the specific binding site on ADRB2 then the signal transduction pathways begins. The three-dimensional configuration of ADRB2 is uniquely and determines by its amino acid sequence. In this study, human ADRB2, dog ADRB2, and cat ADRB2 sequences were studied by sequence of P07550, P54833 and Q9TST5, respectively. The similarity of human ADRB2 and dog ADRB2 was 90% whereas the similarity between human ADRB2 and cat ADRB2 was 89%. In addition, the similarity between dog ADRB2 and cat ADRB2 was 95%. The in silico ADRB2 models were generated and compared among species of interest. The results show that the shapes and the pocket sites of ADRB2 differ between species. The differences of ADRB2 three-dimensional configuration may give explanations about the variety of interaction between ADRB2 and its agonist among human, dog and cat. Further study of protein-protein interaction, structure-based drug design, and novel function of ADRB2 in companion animals may have basis from human ADRB2.engMahidol UniversityADRB2Homology modelingin silicoHumanDogCatJournal of Applied Animal ScienceResearch ArticleFaculty of Veterinary Science Mahidol University