Homology modeling of apoprotein Opsin and covalent docking of 11-cis retinal and 11-cis 3, 4-didehyroretinal to obtain structures of Rhodopsin and Porphyropsin from Zebra danio, Danio rerio (Hamilton, 1822)

Jordan Journal of Biological Sciences

article

Susmita Dey¹  Gitartha Kaushik²  Saurav Mahanta³  Arijit Chakraborty⁴ 

[1] Dept. of Zoology, Royal Global University;Faulty of Science, Assam Downtown University;Bioinformatics Center, National Institute of Electronics and Information Technology;Department of Sports & Exercise Science, Somaiya Sports Academy, Somaiya Vidyavihar University

关键词: Zebra fish;    Opsin;    Rhodopsin;    Porphyropsin;    11-cis retinal;    11-cis 3;    4-didehyroretinal;   

DOI  :  10.54319/jjbs/140413

学科分类：生物科学（综合）

来源: Hashemite University, Deanship of Research and Higher Studies

【 摘 要 】

Opsin proteins are classically seven transmembrane receptor proteins which detect light. The present investigation describes the stereoscopic structure of the apoprotein Opsin by online structure determining tools using the crystallographic structure of Rhodopsin from Bos taurus as the template. The modeled structure was validated and checked through validated data tools for stereochemical quality of a protein structure, ProSa and the square root of the mean square deviation between the templates and the predicted structure was calculated using PyMol. It was found that the chromophores, 11-cis retinal and 11-cis 3, 4-didehydroretinal was covalently docked with apoprotein which gives the structures of Rhodopsin and Porphyropsin respectively. Due to its close homology to the human rhodopsin (accession P08100), zebra fish rhodopsin may serve as an excellent model for study of human diseases in future. This article represents the test of structure/function relationship of apoprotein opsin in this ornamental aquarium fish and provides a foundation for future work exploring cellular and molecular pathways of photoreception in retinal development and disease models.

【 授权许可】

CC BY