Structural Analysis of the Human Interferon γ Receptor: A Small Segment of the Intracellular Domain is Specifically Required for Class I Major Histocompatibility Complex Antigen Induction and Antiviral Activity
Abstract
Mutations of the human interferon gamma (IFN-gamma) receptor intracellular domain have permitted us to define a restricted region of that domain as necessary for both induction of class I major histocompatibility complex antigen by IFN-gamma and protection against encephalomyocarditis virus. This region consists of five amino acids (YDKPH), all of which are conserved in the human and murine receptors. Tyr-457 and His-461 are essential for activity. Approximately 80% of the amino acids of the intracellular domain of the receptor is not required for major histocompatibility complex class I antigen induction or for antiviral protection against encephalomyocarditis virus. The observation that there was no protection by IFN-gamma against vesiculostomatitis virus indicates that other factors, in addition to chromosome 21 accessory factor(s), are required to generate the full complement of transduction signals from the human IFN-gamma receptor.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- December 1992
- DOI:
- 10.1073/pnas.89.23.11317
- Bibcode:
- 1992PNAS...8911317C