JBIC Journal of Biological Inorganic Chemistry

, Volume 18, Issue 2, pp 183–194

Solution structure and dynamics of human S100A14

  • Ivano Bertini
  • Valentina Borsi
  • Linda Cerofolini
  • Soumyasri Das Gupta
  • Marco Fragai
  • Claudio Luchinat
Original Paper

DOI: 10.1007/s00775-012-0963-3

Cite this article as:
Bertini, I., Borsi, V., Cerofolini, L. et al. J Biol Inorg Chem (2013) 18: 183. doi:10.1007/s00775-012-0963-3

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.

Keywords

Nuclear magnetic resonance Binding affinity Protein folding 

Supplementary material

775_2012_963_MOESM1_ESM.pdf (258 kb)
Supplementary material 1 (PDF 258 kb)

Copyright information

© SBIC 2012

Authors and Affiliations

  • Ivano Bertini
    • 1
    • 2
  • Valentina Borsi
    • 1
  • Linda Cerofolini
    • 1
  • Soumyasri Das Gupta
    • 1
  • Marco Fragai
    • 1
    • 2
  • Claudio Luchinat
    • 1
    • 2
  1. 1.Magnetic Resonance Center (CERM)University of FlorenceSesto FiorentinoItaly
  2. 2.Department of ChemistryUniversity of FlorenceSesto FiorentinoItaly

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