Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein

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.

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Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie International Edition 2005-10, Vol.44 (39), p.6341-6344
Hauptverfasser:	Arnesano, Fabio, Banci, Lucia, Bertini, Ivano, Fantoni, Adele, Tenori, Leonardo, Viezzoli, Maria Silvia
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites calcium Calcium - chemistry Carbon Isotopes copper Copper - chemistry Dimerization helical structures Humans Magnetic Resonance Spectroscopy - methods Nitrogen Isotopes NMR spectroscopy Protein Conformation Protein Structure, Tertiary protein structures S100 Proteins - chemistry Structure-Activity Relationship
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Beschreibung
Zusammenfassung:	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.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200500540