1ifa
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THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA
OverviewOverview
The crystal structure of recombinant murine interferon-beta (IFN-beta) has, been solved by the multiple isomorphous replacement method and refined to, an R-factor of 20.5% against 2.6 A X-ray diffraction data. The structure, shows a variant of the alpha-helix bundle with a new chain-folding, topology, which seems to represent a basic structural framework of all the, IFN-alpha and IFN-beta molecules belonging to the type I family., Functionally important segments of the polypeptide chain, as implied, through numerous gene manipulation studies carried out so far, are, spatially clustered indicating the binding site(s) to the receptor(s)., Comparison of the present structure with those of other alpha-helical, cytokine proteins, including porcine growth hormone, interleukin 2 and, interferon gamma, indicated either a topological similarity in chain, folding or a similar spatial arrangement of the alpha-helices.
About this StructureAbout this Structure
1IFA is a Single protein structure of sequence from Mus musculus with ASN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional crystal structure of recombinant murine interferon-beta., Senda T, Shimazu T, Matsuda S, Kawano G, Shimizu H, Nakamura KT, Mitsui Y, EMBO J. 1992 Sep;11(9):3193-201. PMID:1505514
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