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PDBsum entry 1ak7
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Actin depolymerization factor
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PDB id
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1ak7
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References listed in PDB file
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Key reference
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Title
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Tertiary structure of destrin and structural similarity between two actin-Regulating protein families.
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Authors
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H.Hatanaka,
K.Ogura,
K.Moriyama,
S.Ichikawa,
I.Yahara,
F.Inagaki.
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Ref.
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Cell, 1996,
85,
1047-1055.
[DOI no: ]
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PubMed id
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Abstract
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Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various
eukaryotes. We determined the tertiary structure of destrin by triple-resonance
multidimensional nuclear magnetic resonance. In spite of there being no
significant amino acid sequence homology, we found that the folding of destrin
was strikingly similar to that of repeated segments in the gelsolin family,
which resulted in a new protein fold group. Sequential dissimilarity of the
actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent
actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive
phosphoinositide-competitive actin binding, of pH-dependent filament severing,
and of nuclear translocation with actin in response to stresses, are discussed
on the basis of the tertiary structure.
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Figure 3.
Figure 3. Relationship between the Cofilin and Gelsolin
Families(A) Superposition of the mean structures of destrin
(black) and three members of the gelsolin family (red, gelsolin
segment-1; green, villin segment-1; blue, severin segment-2). We
used coordinates provided by [44], Model 1 in Protein Data Bank
entry 1VIL ( [40]), and Protein Data Bank entry 1SVR ( [61]),
respectively. The regions used for superposition are described
in the text and also shown here in bold lines. Start and end
residues of the regions are numbered.(B) Sequence alignments of
destrin and gelsolin family members whose tertiary structures
have been solved. Meaningful residues are colored (green,
hydrophobic; red, acidic; blue, basic). Regular secondary
structure elements are underlined and boxed by colors (yellow,
α helix; light blue, β strand). The sequences of destrin and
gelsolin segment-1 are numbered, and numbering of the latter is
adjusted to the plasma-form corresponding to [44]. Regions used
for the superposition in (A) are represented by dotted lines.
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Figure 4.
Figure 4. Actin Binding by Destrin(A) Model of the complex
of actin (green) and destrin (yellow) made from coordinates of
the complex of actin and gelsolin segment-1 ([44]). Destrin is
superposed on gelsolin segment-1, as shown in Figure 3A, and
gelsolin segment-1 is hidden. The actin-binding helix is colored
red.(B) Assumed actin-binding residues in destrin (top) and
actual actin-binding residues in gelsolin segment-1 (bottom)
elucidated by [44]. Destrin can be related to Figure 2 by
20° y rotation. The two molecules are oriented by the
superposition described in Figure 3A. Molecular surfaces were
produced using the program GRASP ( [51]) and colored according
to amino acid residue type (yellow, hydrophobic; red, acidic;
blue, basic; white, others) instead of usual surface electric
potential.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1996,
85,
1047-1055)
copyright 1996.
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