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Updated: Aug 8, 2026
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Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
Published on: September 29, 2019
Purification, crystallization and preliminary X-ray diffraction of human S100A15
Karen M Boeshans1, Ronald Wolf, Christopher Voscopoulos
1X-ray Crystallography Facility, NIAMS, National Institutes of Health, Bethesda, MD 20892, USA.
Summary
Human S100A15 protein, linked to psoriasis, was crystallized to reveal its structure. This structural insight aids in understanding calcium-binding proteins and may lead to new psoriasis therapies.
Area of Science:
- Biochemistry
- Structural Biology
- Dermatology
Background:
- Human S100A15 is a novel calcium-binding protein identified in psoriasis.
- It is upregulated in lesional skin and implicated in calcium-mediated signal transduction.
- Its role in disease pathogenesis and potential as a therapeutic target are under investigation.
Purpose of the Study:
- To elucidate the structure of human S100A15.
- To understand how S100A15 interacts with target molecules.
- To provide insights into the function of S100A15 in relation to psoriasis.
Main Methods:
- Cloning, expression, and purification of human S100A15 protein.
- Crystallization of S100A15, yielding two crystal forms (triclinic and monoclinic).
- X-ray diffraction analysis to determine crystal structures.
Main Results:
- Two crystal forms of S100A15 were obtained and characterized.
- Form I crystals (triclinic) diffracted to 1.7 angstroms resolution.
- Form II crystals (monoclinic) diffracted to 2.0 angstroms resolution.
Conclusions:
- The structural analysis of S100A15 provides a foundation for understanding its function.
- This research aids in phylogenetic comparisons within the S100 protein family.
- The findings may facilitate the development of targeted therapies for psoriasis.
