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.