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PDBsum entry 1wu3
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References listed in PDB file
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Key reference
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Title
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Refined crystal structure of recombinant murine interferon-Beta at 2.15 a resolution.
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Authors
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T.Senda,
S.Saitoh,
Y.Mitsui.
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Ref.
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J Mol Biol, 1995,
253,
187-207.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of recombinant murine interferon-beta (reMuIFN-beta) has
been refined at 2.15 A resolution using newly collected synchrotron data. Based
on 11,228 reflections (8.0 to 2.15 A), a final R-factor of 19.1% (with a free
R-factor of 25.8%) was obtained with a model obeying standard geometry within
0.013 A in bond lengths and 1.4 degrees in bond angles. Compared with the
previously reported model, several amino acid residues in helix A are
frame-shifted, the conformations are changed for parts of loops AB and BC, helix
C is extended and a new short helix exists in loop CD. Evolutionary
considerations taken together, the type I interferons appear to share common
structural features with respect to the chain-folding topology and the
hydrogen-bond networks between various polypeptide segments. Specifically, the
disposition of the C-terminal segment of loop AB (after Arg33), known to be an
important receptor-binding site, seems to be strictly maintained among the type
I interferons. The exposed amino acid residues on helices A and C, which have
recently been implicated as the binding site for another receptor molecule, are
less well conserved. This may be responsible for varied cellular effects among
the subtypes of type I interferons.
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Figure 5.
Figure 5. Hydrogen-bond networks between various segments. The broken lines represent hydrogen bonds, and the
side-chains playing a key role in the networks are shown as thicker lines. Filled circles marked WAT represent bound water
molecules. Hydrogen-bond networks are shown for the interface (a) between helix A and helix C, (b) that around Arg142
(helix E), (c) that between helix D and helix E and (d) that between loop AB and helix D.
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Figure 7.
Figure 7. Amino acid conservation rate as displayed on the three-dimensional crystal structure of MuIFN-b (the view
direction is approximately the same as in Figure 3). (a) Front view with the hot area in top front. (b) Back view. Amino
acid residues more than 80% conserved among the type I interferons are colored red, while those having a conservation
ratio between 60 and 80% are colored yellow. The other, less conserved residues are colored white.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
253,
187-207)
copyright 1995.
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Secondary reference #1
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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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Secondary reference #2
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Title
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Three-Dimensional structure of recombinant murine interferon-Beta
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Authors
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T.Senda,
S.Matsuda,
H.Kurihara,
K.T.Nakamura,
G.Kawano,
H.Shimizu,
H.Mizuno,
Y.Mitsui.
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Ref.
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proc jpn acad ,ser b, 1990,
66,
77.
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Secondary reference #3
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Title
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Structural, Functional and evolutionary implications of the three-Dimensional crystal structure of murine interferon-Beta.
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Authors
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Y.Mitsui,
T.Senda,
T.Shimazu,
S.Matsuda,
J.Utsumi.
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Ref.
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Pharmacol Ther, 1993,
58,
93.
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PubMed id
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