1. Solution structure and dynamics of human S100A14
- Author
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Linda Cerofolini, Ivano Bertini, Valentina Borsi, Claudio Luchinat, Soumyasri Das Gupta, and Marco Fragai
- Subjects
Models, Molecular ,Light ,Protein family ,Surface Properties ,chemistry.chemical_element ,Calcium ,Biochemistry ,Protein Structure, Secondary ,RAGE (receptor) ,Inorganic Chemistry ,03 medical and health sciences ,Glycation ,Humans ,Scattering, Radiation ,Protein Structure, Quaternary ,Receptor ,Nuclear Magnetic Resonance, Biomolecular ,Histidine ,030304 developmental biology ,0303 health sciences ,Binding Sites ,Binding protein ,Calcium-Binding Proteins ,030302 biochemistry & molecular biology ,Protein Structure, Tertiary ,3. Good health ,Zinc ,chemistry ,Protein folding ,Apoproteins ,Copper ,Protein Binding - Abstract
Human S100A14 is a member of the EF-hand calcium-binding protein family that has only recently been described in terms of its functional and pathological properties. The protein is overexpressed in a variety of tumor cells and it has been shown to trigger receptor for advanced glycation end products (RAGE)-dependent signaling in cell cultures. The solution structure of homodimeric S100A14 in the apo state has been solved at physiological temperature. It is shown that the protein does not bind calcium(II) ions and exhibits a "semi-open" conformation that thus represents the physiological structure of the S100A14. The lack of two ligands in the canonical EF-hand calcium(II)-binding site explains the negligible affinity for calcium(II) in solution, and the exposed cysteines and histidine account for the observed precipitation in the presence of zinc(II) or copper(II) ions.
- Published
- 2012
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