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Issue 22, 2011
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NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

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Abstract

The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.

Graphical abstract: NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

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Article information


Submitted
20 Mar 2011
Accepted
18 Apr 2011
First published
09 May 2011

Chem. Commun., 2011,47, 6407-6409
Article type
Communication

NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine

M. S. Shoshan, D. E. Shalev, W. Adriaens, M. Merkx, T. M. Hackeng and E. Y. Tshuva, Chem. Commun., 2011, 47, 6407
DOI: 10.1039/C1CC11600B

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