Publication: Preliminary report: Homology Modeling of human, dog and catβ-adrenergic receptors
3
Issued Date
2012
Resource Type
Language
eng
ISSN
1906-2257
Rights
Mahidol University
Rights Holder(s)
Faculty of Veterinary Science Mahidol University
Bibliographic Citation
Journal of Applied Animal Science. Vol.5, No.2 (2012), 35-42
Suggested Citation
Waraphan Toniti, Pranom Puchadapirom, Aekkapot Chamkasem, Tawewan Tansatit Preliminary report: Homology Modeling of human, dog and catβ-adrenergic receptors. Journal of Applied Animal Science. Vol.5, No.2 (2012), 35-42. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/13319
Research Projects
Organizational Units
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Journal Issue
JAAS Vol. 5 No. 2
(2555)
Thesis
Title
Preliminary report: Homology Modeling of human, dog and catβ-adrenergic receptors
Alternative Title(s)
การทดลองเบื้องต้น: การสร้างแบบจำลองของตัวรับอะดรีเนอร์จิกชนิดเบต้าในมนุษย์ สุนัข และแมว โดยใช้เทคนิค Homology Modeling
Abstract
Beta 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.