Cap43 has been reported to be specifically induced by nickel compounds in a variety of cell lines. Its function is not yet clear, but Cap43 protein does appear to be inducec in response to an increase in intracellular concentration of Ca2+, caused by nickel ion exposure in cultured human cells. Cap43 is expressed at low levels in normal tissues. However, in a variety of cancers, it is overexpressed in cancer cells.The peculiarity of Cap43 is its mono-histidinic motif consisting of ten amino acids (TRSRHTSEG) repeated three times in the C-terminus.We have analyzed, for Ni(II) binding, the 30-amino acid C-terminal sequence of the protein, TRSRSHTSEG-TRSRTHTSEG-TRSRSHTSEG, by the use of different NMR techniques such as 1D, NOESY, TOCSY and ROESY experiments. From the data thus collected we calculated a model of the structure for the peptide-Ni(II) complex, confirming the characteristic binding of a nickel ion to each 10-amino acid fragment and showing the interesting structural changes the peptide undergoes upon metal coordination.

An NMR study on nickel binding to Cap43 protein / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella. - (2006), pp. 405-405. (Intervento presentato al convegno SCI 2006: 22. Congresso nazionale della Società Chimica Italiana: atti del congresso).

An NMR study on nickel binding to Cap43 protein

Zoroddu, Maria Antonietta;Peana, Massimiliano Francesco;Medici, Serenella
2006-01-01

Abstract

Cap43 has been reported to be specifically induced by nickel compounds in a variety of cell lines. Its function is not yet clear, but Cap43 protein does appear to be inducec in response to an increase in intracellular concentration of Ca2+, caused by nickel ion exposure in cultured human cells. Cap43 is expressed at low levels in normal tissues. However, in a variety of cancers, it is overexpressed in cancer cells.The peculiarity of Cap43 is its mono-histidinic motif consisting of ten amino acids (TRSRHTSEG) repeated three times in the C-terminus.We have analyzed, for Ni(II) binding, the 30-amino acid C-terminal sequence of the protein, TRSRSHTSEG-TRSRTHTSEG-TRSRSHTSEG, by the use of different NMR techniques such as 1D, NOESY, TOCSY and ROESY experiments. From the data thus collected we calculated a model of the structure for the peptide-Ni(II) complex, confirming the characteristic binding of a nickel ion to each 10-amino acid fragment and showing the interesting structural changes the peptide undergoes upon metal coordination.
2006
An NMR study on nickel binding to Cap43 protein / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella. - (2006), pp. 405-405. (Intervento presentato al convegno SCI 2006: 22. Congresso nazionale della Società Chimica Italiana: atti del congresso).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/261539
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