Please use this identifier to cite or link to this item: http://localhost:80/xmlui/handle/123456789/13133
Title: Molecular structure and functions of zinc binding metallothionein-1 protein in mammalian body system
Authors: Hongfang, Guo
Guanghui, Cui
Khan, Rajwali
Huanxia, Jia
Jianxin, Zhang
Haidar Abbas Raza, Sayed
Ayaz, Muhammad
Shafiq, Muhammad
Zan, Linsen
Keywords: Zinc
metalloenzymes
metallothionein
zinc finger motif
transcription factors
conserved motifs of MT-1 protein
Issue Date: 4-Aug-2020
Publisher: Karachi:Pakistan Journal of Pharmaceutical Sciences, university of Karachi.
Citation: Molecular structure and functions of zinc binding metallothionein-1 protein in mammalian body system
Abstract: Zinc a major trace element; perform diverse roles in genetics and physiology in almost every vital body system of the mammalian body. Zinc regulates the expression of almost all essential genes responsible for performing pivotal functions in mammal cells through provision of structural integrity to the major transcriptional factors Zn finger Proteins (ZnF) and gene regulation for production of metallothionein protein. Zinc performed at least eight vital functions in living organisms including gene regulation e.g., as a promoter through metal response elements, structural i.e. zinc-finger motifs, catalytic e.g., metalloenzymes, DNA and RNA polymerase, DNA replication, Growth promotion, antioxidant, regulate functions of central nervous system and also act as hepato-protectant and detoxifying agent. Almost all of these vital functions are regulated through metallothionein protein, a cysteine rich Zn binding protein. These functions are basic mechanism for sustaining life. Therefore, this review paper was planned with the objective to highlight the important functions of Zn inside the mammal‟s body with particular reference to the metallothionein protein. Bioinformatics study performed for estimation of conservation and evolution of this important protein shows its greater conservancies in six important mammalian species.
URI: http://142.54.178.187:9060/xmlui/handle/123456789/13133
ISSN: 1011-601X
Appears in Collections:Issue 4

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