1FG9
3:1 COMPLEX OF INTERFERON-GAMMA RECEPTOR WITH INTERFERON-GAMMA DIMER
Summary for 1FG9
Entry DOI | 10.2210/pdb1fg9/pdb |
Descriptor | INTERFERON GAMMA, INTERFERON-GAMMA RECEPTOR ALPHA CHAIN (2 entities in total) |
Functional Keywords | cytokine-receptor complex, fibronectin type-iii, immune system |
Biological source | Homo sapiens (human) More |
Cellular location | Secreted: P01579 Membrane; Single-pass type I membrane protein: P15260 |
Total number of polymer chains | 5 |
Total formula weight | 114410.07 |
Authors | Thiel, D.J.,le Du, M.-H.,Walter, R.L.,D'Arcy, A.,Chene, C.,Fountoulakis, M.,Garotta, G.,Winkler, F.K.,Ealick, S.E. (deposition date: 2000-07-28, release date: 2000-08-11, Last modification date: 2024-10-30) |
Primary citation | Thiel, D.J.,le Du, M.H.,Walter, R.L.,D'Arcy, A.,Chene, C.,Fountoulakis, M.,Garotta, G.,Winkler, F.K.,Ealick, S.E. Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex. Structure Fold.Des., 8:927-936, 2000 Cited by PubMed Abstract: Molecular interactions among cytokines and cytokine receptors form the basis of many cell-signaling pathways relevant to immune function. Interferon-gamma (IFN-gamma) signals through a multimeric receptor complex consisting of two different but structurally related transmembrane chains: the high-affinity receptor-binding subunit (IFN-gammaRalpha) and a species-specific accessory factor (AF-1 or IFN-gammaRbeta). In the signaling complex, the two receptors probably interact with one another through their extracellular domains. Understanding the atomic interactions of signaling complexes enhances the ability to control and alter cell signaling and also provides a greater understanding of basic biochemical processes. PubMed: 10986460DOI: 10.1016/S0969-2126(00)00184-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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