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PDBsum entry 7dsa
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Cytosolic protein
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PDB id
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7dsa
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Contents |
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264 a.a.
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239 a.a.
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117 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural insights into the regulation of actin capping protein by twinfilin c-Terminal tail.
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Authors
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S.Takeda,
R.Koike,
I.Fujiwara,
A.Narita,
M.Miyata,
M.Ota,
Y.Maéda.
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Ref.
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J Mol Biol, 2021,
433,
166891-166891.
[DOI no: ]
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PubMed id
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Abstract
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Twinfilin is a conserved actin regulator that interacts with actin capping
protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity
with the CP interaction (CPI) motif of CARMIL. Here we report the crystal
structure of TWtail in complex with CP. Our structure showed that although
TWtail and CARMIL CPI bind CP to an overlapping surface via their middle
regions, they exhibit different CP-binding modes at both termini. Consequently,
TWtail and CARMIL CPI restrict the CP in distinct conformations of open and
closed forms, respectively. Interestingly, V-1, which targets CP away from the
TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a
stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which
rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique
CP-binding motif that regulates CP in a manner distinct from CARMIL CPI.
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