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Structural elements required for receptor recognition of human interferon-gamma

D L Lundell¹, S K Narula

¹Schering-Plough Research Institute, Kenilworth, NJ 07033.

Pharmacology & Therapeutics

|October 1, 1994

Summary

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Interferon (IFN)-gamma is crucial for immune responses. Its structure reveals three key regions involved in binding to its receptor, forming a potential continuous binding domain.

Area of Science:

Immunology and Molecular Biology
Protein Structure and Function

Background:

Interferon (IFN)-gamma plays a vital role in various immune responses.
Recent elucidation of the three-dimensional structure of human and rabbit IFN-gamma provides new insights.

Purpose of the Study:

To integrate structural and functional data of IFN-gamma.
To develop a working model for IFN-gamma:receptor interaction.

Main Methods:

Analysis of mutagenesis studies.
Corroboration using peptides, antibodies, and proteolytic digestion.

Main Results:

Identification of three critical regions for receptor binding: a loop between helices A and B, His111 in helix F, and the flexible carboxyl terminus.

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These regions may collectively form a single, continuous binding domain.

Conclusions:

The identified regions are essential for IFN-gamma receptor interaction.
A structural model for IFN-gamma binding is proposed, integrating diverse experimental evidence.