2lag
From Proteopedia
Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY
Structural highlights
FunctionINAR2_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.[1] [2] [3] [4] [5] Publication Abstract from PubMedNMR 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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