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Title
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Three-dimensional crystal structure of recombinant murine interferon-beta.
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Authors
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T.Senda,
T.Shimazu,
S.Matsuda,
G.Kawano,
H.Shimizu,
K.T.Nakamura,
Y.Mitsui.
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Ref.
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Embo J, 1992,
11,
3193-3201.
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PubMed id
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Abstract
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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.
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