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Umesh C. Metal ions are integral part of some viral proteins and play an important role in their survival and pathogenesis.

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Zinc, magnesium and copper are the Graduation College Program metal ion that binds with viral proteins. Metal ions participate in maturation of genomic RNA, activation and catalytic mechanisms, reverse transcription, initial integration process and protection of newly synthesized DNA, inhibition of proton translocation M2 proteinminus- and plus-strand transfer, enhance nucleic acid annealing, activation of transcription, integration of viral DNA into specific sites and act as a chaperone of nucleic acid. In certain situations more than one metal ion is required e.

This review underscores the importance of metal ions in the survival and pathogenesis of a large group of viruses and studies on structural basis for metal binding should prove useful in the early Protein Structure And Proteins Proteins and development of viral inhibitors. Among the many roles of metal ions in biological processes are bridging distant residues or domains of proteins, mediating interactions between proteins and ligands, and serving in the active site as a nucleophilic catalyst and in transfer of electron.

Biological processes are often metal ion specific, although more than one metal ion can play each of these roles. The conformational changes induced by binding a metal ion are remarkable. A number of trace metals are essential micronutrients and their deficiency and infectious diseases often coexist and exhibit complex interactions. Several trace metals such as Protein Structure And Proteins Proteins, copper and manganese, etc. Deficiency of trace metals is known to alter the genome of the viruses and the grave consequences of this may be the emergence of new infections [3].

On the other hand some metals like hexavalent chromium may have toxic effects 45]. Metals are integral part of several viruses and are known to play an important role in their survival and pathogenesis.

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This paper briefly reviews the consequences of the interactions of various metal ions with proteins of different viruses. Due to constraint of space only a limited number of studies have been Protrins. Viruses are the smallest infectious agents containing only one type of nucleic acid DNA or RNA covered by a protein coat, which may be surrounded by a Protdin membrane. A virion is composed of viral proteins, nucleic acid, lipids and carbohydrates. The structural proteins of viruses protect the viral genome, participate in attachment of virus to a susceptible cell, facilitate transfer of viral nucleic acid from one Protein Structure And Proteins Proteins cell to another and are antigenic determinants of the virus.

Viral envelopes contain lipids and glycoproteins gpthe lipids are derived from the here cell while the glycoproteins are virus-encoded. Surface glycoproteins attach the virus to a target cell and are important viral antigens. Viral proteins coded by nonstructural genes are known as nonstructural proteins See more. Present in the virus-infected cells, these proteins appear to have regulatory roles during replication. The mature structural proteins are C, E1 and E2 [6]. An interaction between a protein and a Protein Structure And Proteins Proteins ion is of different types.

Metalloprotein is a generic term for a protein that also contains a metal cofactor.

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Portein The metal ions in metalloproteins are critical to the protein's function, structure, or stability and numerous essential biological functions [7]. Understanding and ultimately controlling the binding and activity of protein metal sites are of great biological and medical importance. The functions of metalloproteins having metals that bind with different viral proteins are presented in Table 1. Modified from Chaturvedi et al. The commonest metal to bind with a virus-protein is zinc. Zinc is the second most abundant trace metal found in eukaryotic Protein Structure And Proteins Proteins, second only to iron. Zinc is required for essential catalytic functions in more than enzymes, stabilization and induction of the folding of protein subdomains.

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The latter Protein Structure And Proteins Proteins include the essential role of zinc in the folding of the DNA-binding domains of eukaryotic transcription factors, including the ZF transcription factors [9]. ZF are small protein domains in which zinc plays a structural role contributing to the stability of the domain and are small DNA-binding peptide motifs. The cysteine-rich zinc-binding motifs known as the RING and B-box are found in several unrelated proteins. ZF are structurally diverse and are present among proteins that perform a broad range of functions in various cellular processes, such as replication and repair, transcription and translation, metabolism and signaling, cell proliferation and apoptosis.

ZF typically function as interaction modules and bind to a wide variety of compounds, such as nucleic acids, proteins and small molecules. Three of these fold groups comprise the majority of zinc fingers, namely, C2H2-like finger, treble clef finger and the zinc ribbon [10].]