2lag | pdb_00002lag

Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY

spinqualitylabelsall models 2lag, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lag is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1kz1 Gene: IFNAR2, IFNABR, IFNARB (HUMAN), IFNA2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [INAR2_HUMAN] Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. [IFNA2_HUMAN] Produced by macrophages, IFN-alpha have antiviral activities. Publication Abstract from PubMed NMR detection of intermolecular interactions between protons in large protein complexes is very challenging since it is difficult to distinguish between weak NOEs from intermolecular interactions and the much larger number of strong intramolecular NOEs. This challenging task is exacerbated by the decrease in signal-to-noise ratio in the often used isotope-edited and isotope-filtered experiments as a result of enhanced T2 relaxation. Here we calculate a double difference spectrum that shows exclusively intermolecular NOEs and manifests the good signal-to-noise ratio in 2D homonuclear NOESY spectra even for large proteins. The method is straightforward and results in a complete picture of all intermolecular interactions involving non exchangeable protons. Ninety seven such 1H-1H NOEs were assigned for the 44 KDa interferon-alpha2/IFNAR2 complex and used for docking these two proteins. The symmetry of the difference spectrum, its superb resolution and unprecedented signal-to-noise ratio in this large protein/receptor complex suggest that this method is generally applicable to study large biopolymeric complexes. Observation of intermolecular interactions in large protein complexes by 2D-double difference NOESY: application to the 44 kDa interferon-receptor complex.,Nudelman I, Akabayov SR, Scherf T, Anglister J J Am Chem Soc. 2011 Aug 8. PMID:21819146 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Interferon 3D structures Interferon receptor 3D structures Multiple sclerosis

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