COMPARATIVE MODELLING AND DOCKING STUDIES OF CYTOCHROME C OXIDASE SUBUNIT 1 PROTEINAbstract
Cytochrome c oxidase, a mitochondrial metalloenzyme acting as the terminal enzyme of the mitochondrial respiratory chain. It provides a critical function in cellular respiration in both eukaryotes and prokaryotes. The recent development in technology has enabled researchers to understand the genetic, molecular, structural, and functional properties of proteins to identify appropriate targets against diseases, and as a result, many anti-inflammatory and anti-proliferative drugs have been developed. In the absence of X-ray and NMR protein crystal structure, homology modeling provides a useful 3D model for a protein that is related to at least one known protein structure. In the present study, the 3D molecular structures of nine Cytochrome c oxidase subunit 1 protein from different species such as Myxine glutinosa, Struthio camelus, Sus scrofa, Homo sapiens, Xenopus laevis, Halichoerus grypus, Zygogeomys trichopus, Buteo buteo, and Plasmodium falciparum were predicted using homology modeling software MODDLLER. The modeled structures were docked using Autodock4.2 software with ten different natural compounds and three drugs as a control to study the molecular interactions of these compounds with the coat protein. The results show that all the compounds exhibited good interactions with modeled proteins.
V. Mallojala, K. Pasam, S. K. Gunda *, S. Bandi and M. Shaik
Bioinformatics Division, PGRRCDE, Osmania University, Hyderabad, Telangana, India.
31 October 2019
26 February 2020
20 March 2020
01 October 2020