The Structure of Interferon Gamma

1. The Structure of Interferon Gamma The most significant (IFNG ELISA) advances in our understanding of interferon- have been made in the year in the elucidation of the molecule's three- dimensional structure and the analysis of the molecular structure and functional domains of the interferon- receptor. The immunoregulatory role of interferon- has been better established in research dealing with its effects on B-cell activity and its production by diverse T-cell subsets, and a clearer understanding of the molecular processes of gene activation by interferon- has been gained. Multiple-isomorphous-replacement approaches have been used to determine the x-ray crystal structure of recombinant human interferon-gamma. In the asymmetric unit, interferon-gamma, which is dimeric in solution, crystallizes as two dimers linked by a noncrystallographic twofold axis. The protein is predominantly alpha-helical, with six helices making up around 62 percent of the structure in each subunit; there is no beta-sheet. The intertwining of helices across the subunit interface, together with various intersubunit interactions, stabilizes the dimeric structure of human interferon-gamma. The six-helical core of the IFN (IFNG ELISA) gamma monomer is surrounded by a prolonged unfolded sequence at the C-terminal region. The -helices in the structure's core are numbered 1 through 6. The antiparallel interlocking of the two monomers forms the physiologically active dimer. How interferon Gamma is regulated? There is evidence that a pseudoknotted domain in interferon-gamma 5' UTR regulates its expression. There's also evidence that microRNAs like miR-29 influence interferon-gamma, either directly or indirectly. Furthermore, there is evidence that GAPDH regulates interferon-gamma expression in T-cells. This interaction occurs in the 3'UTR, where GAPDH binding stops the mRNA region from being translated.