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Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

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Solution structure and dynamics of human S100A14.

Ivano Bertini^1,2, Valentina Borsi¹, Linda Cerofolini¹

¹Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry

|December 1, 2012

Summary

Human S100A14 protein, involved in tumor progression, does not bind calcium ions. Its physiological structure is semi-open, explaining its behavior in various conditions.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Human S100A14 is an EF-hand calcium-binding protein family member with emerging roles in pathology.
S100A14 is overexpressed in various tumor cells and can trigger receptor for advanced glycation end products (RAGE)-dependent signaling.

Purpose of the Study:

To determine the solution structure of homodimeric S100A14 at physiological temperature.
To elucidate the calcium-binding properties and structural conformation of S100A14 in its apo state.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy to solve the solution structure.
Structural analysis to identify calcium-binding sites and conformational states.

Main Results:

The solution structure of homodimeric S100A14 in the apo state was determined at physiological temperature.
S100A14 does not bind calcium(II) ions, exhibiting a "semi-open" conformation.
The protein's EF-hand site lacks canonical ligands for calcium binding, resulting in negligible affinity.
Exposed cysteines and histidine residues contribute to precipitation with zinc(II) or copper(II) ions.

Conclusions:

The determined "semi-open" conformation represents the physiological structure of S100A14.
S100A14's inability to bind calcium ions is structurally explained by its EF-hand motif.
The protein's reactivity with divalent metal ions like zinc and copper is linked to its exposed residues.