Structural elements required for receptor recognition of human interferon-gamma.
Interferon (IFN)-gamma is a central factor in numerous immune responses. Recently the three-dimensional structure of human and rabbit IFN-gamma has been elucidated. This review attempts to bring together the structure and function information into a working model of IFN-gamma: receptor interaction. Based on mutagenesis studies, and corroborated by work with peptides, antibodies and proteolytic digestion, three regions have been found to be important for receptor binding: a long loop connecting the A and B helices, His111 in the F helix and a conserved section of the flexible carboxyl terminus. These three regions may form one continuous binding domain.
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Schering-Plough Research Institute, Kenilworth, NJ 07033.
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D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000502:physiology; D001665:Binding Sites; D000939:Epitopes; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010455:Peptides / Q000737:chemistry / Q000502:physiology; D011487:Protein Conformation; D017471:Receptors, Interferon / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000906:Antibodies; D000939:Epitopes; D010455:Peptides; D017471:Receptors, Interferon; D007371:Interferon-gamma