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Updated: Jul 31, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Homology model for oncostatin M based on NMR structural data
D Kitchen1, R C Hoffman, F J Moy
1Immunex Corporation, Seattle, Washington 98101, USA.
This study presents a homology model for Oncostatin M (OM), a cytokine regulating cell growth. The model was built using structural data from related proteins due to the lack of direct OM structural information.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Oncostatin M (OM) is a cytokine involved in cell proliferation and differentiation.
- OM belongs to a protein family characterized by a four-helix bundle fold and disulfide bonds.
- Direct structural data (X-ray or NMR) for OM is currently unavailable.
Purpose of the Study:
- To develop a homology model for Oncostatin M (OM).
- To provide insights into OM's structure in the absence of experimental data.
Main Methods:
- Homology modeling was employed using X-ray structures of related proteins: human growth hormone (hGH), leukemia inhibitory factor (LIF), and granulocyte-colony stimulating factor (G-CSF).
- Alignment for modeling was based on secondary structure, not sequence.
- Nuclear Magnetic Resonance (NMR) data determined OM's secondary structure.
- The homology model was refined using NMR-derived restraints (NOE distances, chemical shift) and a conformational database.
Main Results:
- A refined homology model for Oncostatin M was successfully generated.
- The model incorporates secondary structure information from NMR and experimental structures of related cytokines.
- Refinement utilized NOE distance restraints and chemical shift data.
Conclusions:
- The developed homology model provides a structural representation of Oncostatin M.
- This model serves as a valuable tool for understanding OM's function and interactions.
- Further structural studies can validate and refine this computational model.
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