This work was supported by the European Commission (SPINE contract QLG2-CT-2002-00988). The Italian MURST COFIN03 is acknowledged for financial support.
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Communication
Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein†
Article first published online: 7 SEP 2005
DOI: 10.1002/anie.200500540
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Arnesano, F., Banci, L., Bertini, I., Fantoni, A., Tenori, L. and Viezzoli, M. S. (2005), Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein. Angew. Chem. Int. Ed., 44: 6341–6344. doi: 10.1002/anie.200500540
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Publication History
- Issue published online: 30 SEP 2005
- Article first published online: 7 SEP 2005
- Manuscript Revised: 8 JUN 2005
- Manuscript Received: 13 FEB 2005
Keywords:
- calcium;
- copper;
- helical structures;
- NMR spectroscopy;
- protein structures
New binding sites: Calcium(II) binding to the dimeric protein S100A13 triggers key conformational changes, thus creating two symmetrical copper(II)-binding sites between the helices of the monomers (see picture). These solvent-exposed binding sites are unique among the S100 proteins.