Title : Crystal structure of human interferon-γ
receptor 2 2 reveals the structural basis for
receptor specificity
Abstract :
- Interferon-γ receptor 2 2 is a cell-surface receptor that is required for interferon-γ signalling and therefore plays a critical immunoregulatory role in innate and adaptive immunity against viral and also bacterial and protozoal infections
- A crystal structure of the extracellular part of human interferon-γ receptor 2 2 (IFNγR 2 ) was solved by molecular replacement at 1.8 Å resolution
- Similar to other class 2 receptors , IFNγR 2 has two fibronectin type III domains
- The characteristic structural features of IFNγR 2 are concentrated in its N-terminal domain : an extensive π-cation motif of stacked residues KWRWRH, a NAG-W- NAG sandwich (where NAG stands for N-acetyl-D-glucosamine) and finally a helix formed by residues 78-85, which is unique among class 2 receptors
- Mass spectrometry and mutational analyses showed the importance of N-linked glycosylation to the stability of the protein and confirmed the presence of two disulfide bonds
- Structure-based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon-γ and receptor 1 1 , the ligands of IFNγR 2