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Updated: Aug 11, 2026
11:44
A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
Conserved transactivation domain shared by interferon regulatory factors and Smad morphogens
1Department of Computational Sciences, Axys Pharmaceuticals, La Jolla, CA 92037, USA.
Journal of Molecular Medicine (Berlin, Germany)
|July 30, 1999
Summary
Interferon regulatory factors (IRFs) interact with other proteins. A specific loop, similar to Smad4
Area of Science:
- Molecular biology
- Genetics
- Protein interactions
Background:
- Interferon regulatory factors (IRFs) control the expression of interferon-inducible genes and interferons.
- IRFs possess N-terminal DNA-binding domains and C-terminal domains homologous to Smad proteins.
Purpose of the Study:
- To investigate the structural basis of protein-protein interactions mediated by IRF C-terminal domains.
- To compare IRF C-terminal domains with Smad proteins involved in transforming growth factor signaling.
Main Methods:
- Sequence alignment of IRF and Smad C-terminal domains.
- Structural comparison using the known 3D structure of human Smad4.
Main Results:
- A conserved loop, analogous to Loop 3 in Smad4, was identified in IRFs.
- This conserved loop is suggested to be a key determinant for protein-protein interactions in IRFs.
Conclusions:
- The findings provide insights into the structural mechanisms governing IRF-mediated protein interactions.
- This conserved loop may represent a critical interaction interface for IRF function in gene regulation.
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