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  1. Metalloprotein
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  3. Introduction
  4. Prediction of Metal Ion–Binding Sites in Proteins Using the Fragment Transformation Method
  5. Metal Sites in Proteins and Models - Iron Centres | H.A.O. Hill | Springer

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This item doesn't belong on this page. The zinc atom is not directly involved in catalysis but rather may have a structural role. A similar metal binding motif is found in 2A proteinases of enteroviruses and rhinoviruses, suggesting that they are structurally related [55]. Rotaviruses have a complex architecture. Its double-stranded RNA genome is composed of 11 segments that codes for 6 structural proteins and 6 NS. Several NS facilitate the subsequent processes of genome replication and packaging [65].

The wild-type VP6 depleted of the zinc behaves like the mutant protein and its susceptibility to proteases is greatly increased in the absence of zinc [66]. NS1 synthesized in rotavirus-infected cells binds IRF Rotavirus mRNAs are capped but not polyadenylated, and viral proteins are translated by the cellular translation machinery.

The cellular protein, named RoXaN rotavirus X protein associated with NS3 , contains a minimum of three regions predicted to be involved in protein—protein or nucleic acid—protein interactions. In the carboxy terminus, at least five ZF motifs are observed, suggesting the capacity of RoXaN to bind other proteins or nucleic acids.

RoXaN is capable of interacting with NS3 in vivo and during rotavirus infection and has been implicated in translation regulation [37]. The nucleotide sequences for the simian rotavirus SA11 gene segment 5 codes for the NS There is a conserved region between amino acids 37—81 which contains a generalized motif for a metal binding domain.

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All eight cysteine and two histidine residues in this short sequence are conserved between the simian and bovine NS53 [67]. The conservation of this domain despite extensive sequence diversity in the remainder of the protein suggests that this region is functionally important. Brottier et al. Although a wealth of information has been accumulated on metal-dependent enzymes and proteins, many questions remain. For example, it is not clear why metal ions tends to bind to viral nucleic acids indirectly via a water molecule whereas it tends to bind to proteins directly.

The factors that define the energetically most favorable ligand coordination set and geometry for a given metal cation are ill defined. How does a viral protein select a specific metal cation from the mixture of ions in the surrounding fluids, for example why viral proteins and nucleoproteins choose mostly zinc ions? Is this selectivity due to i the natural abundance of the metal in the biological locality, or ii properties of the metal e.

Most of the studies have been done with zinc. There is a need to study interaction of various other metals with different viral proteins. Stray efforts have been made to use these approaches for the development of antiviral agents. A deeper understanding of these questions and lot more studies on structural basis for metal binding should prove useful in the early design and development of viral inhibitors that may lead to new drug discovery. Professor U. Chaturvedi was formerly Head of the Department of Microbiology at K. UCC is grateful to Dr. Oxford University Press is a department of the University of Oxford.

It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide. Sign In or Create an Account. Sign In. Advanced Search. Article Navigation. Close mobile search navigation Article Navigation. Volume Article Contents. Interaction of viral proteins with metal ions: role in maintaining the structure and functions of viruses Umesh C. Oxford Academic. Google Scholar. Richa Shrivastava. Cite Citation. Permissions Icon Permissions.


Abstract Metal ions are integral part of some viral proteins and play an important role in their survival and pathogenesis. Table 1. Open in new tab. Table 2.

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Open in new tab Download slide. A joint ab initio and molecular mechanics investigation of polycoordinated Zn II complexes with model hard and soft ligands. Variations of the binding energy and of its components with the number and the charges of the ligands. Search ADS. Various cells of immune system and intestine differ in their capacity to reduce hexavalent chromium. Google Preview. GLI activates transcription through a herpes simplex viral protein like activation domain.

Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. A system of protein target sequences for anti-RNA-viral chemotherapy by a vitamin B6-derived zinc-chelating trioxa-adamantane-triol. Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer. The metal binding site of the hepatitis C virus NS3 protease. A spectroscopic investigation. The zinc ring finger in the bICP0 protein encoded by bovine herpesvirus-1 mediates toxicity and activates productive infection.

The vaccinia virus superoxide dismutase-like protein A45R is a virion component that is nonessential for virus replication.

Prediction of Metal Ion–Binding Sites in Proteins Using the Fragment Transformation Method

The rubella virus nonstructural protease requires divalent cations for activity and functions in trans. Cu II inhibition of the proton translocation machinery of the influenza A virus M2 protein. Zinc- and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1. A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1—RNA interaction. Zinc-binding of the cysteine-rich domain encoded in the open reading frame of M1B of the RNA polymerase gene of coronavirus.

Metal Sites in Proteins and Models - Iron Centres | H.A.O. Hill | Springer

Metal thiolate coordination in the E7 proteins of human papilloma virus 16 and cottontail rabbit papilloma virus as expressed in Escherichia coli. Chelating agents stabilize the monomeric state of the zinc binding human papillomavirus 16 E6 oncoprotein. Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion.

Differing roles of the N- and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing. Mutations in the N-terminal domain of human immunodeficiency Virus type 1 nucleocapsid protein affect virion core structure and proviral DNA synthesis. De Guzman. Specific zinc-finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function. Polysulfonates derived from metal thiolate complexes as inhibitors of HIV-1 and various other enveloped viruses in vitro.

Human immunodeficiency virus type 1 Tat protein directly activates neuronal N -methyl-d-aspartate receptors at an allosteric zinc-sensitive site. Role of the histidine residues of visna virus nucleocapsid protein in metal ion and DNA binding.

Shop Books. Add to Wishlist. USD Overview Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual "entatic" are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? And if they are special, how do polypeptide chains and co-factors control this?