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Intermolecular homologies of human interferon-alpha
F E Romantsev1, N N Khodarev, I I Votrin
1Center of Medical Biotechnology, Moscow, Russia.
Biochemical and Biophysical Research Communications
|July 15, 1992
Summary
Human interferon-alpha 2 (IFN) possesses four distinct domains enabling homology pairing with other proteins. These structural features suggest IFN may directly influence DNA functioning within cell nuclei.
Area of Science:
- Molecular Biology
- Structural Biology
- Bioinformatics
Background:
- Human interferon-alpha 2 (IFN) is a crucial cytokine involved in immune responses.
- Understanding the structural basis of IFN's function is key to its therapeutic applications.
Purpose of the Study:
- To identify conserved domains within the human interferon-alpha 2 (IFN) molecule.
- To investigate potential mechanisms by which IFN interacts with cellular components, specifically DNA.
Main Methods:
- Homology search using computer programs.
- Analysis of protein primary structures against extensive databases.
- Examination of tertiary structure models of IFN.
Main Results:
- Identified four domains (residues 35-56, 72-85, 97-110, 124-136) in IFN with high homology-pairing potential.
- These domains are located primarily between alpha-helical cylinders in the tertiary structure.
- Discovered amino acid motifs within IFN suggesting direct interaction with DNA functioning.
Conclusions:
- The identified domains contribute to IFN's ability to interact with diverse proteins.
- IFN's structure includes motifs that may enable direct modulation of DNA processes in the nucleus.
- These findings provide structural insights into IFN's multifaceted biological activities.