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PDBsum entry 5afu
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Motor protein
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PDB id
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5afu
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Contents |
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361 a.a.
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350 a.a.
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275 a.a.
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(+ 2 more)
370 a.a.
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370 a.a.
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369 a.a.
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275 a.a.
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270 a.a.
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587 a.a.
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65 a.a.
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87 a.a.
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168 a.a.
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165 a.a.
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243 a.a.
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52 a.a.
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48 a.a.
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71 a.a.
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31 a.a.
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20 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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The structure of the dynactin complex and its interaction with dynein.
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Authors
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L.Urnavicius,
K.Zhang,
A.G.Diamant,
C.Motz,
M.A.Schlager,
M.Yu,
N.A.Patel,
C.V.Robinson,
A.P.Carter.
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Ref.
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Science, 2015,
347,
1441-1446.
[DOI no: ]
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PubMed id
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Abstract
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Dynactin is an essential cofactor for the microtubule motor cytoplasmic
dynein-1. We report the structure of the 23-subunit dynactin complex by
cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how
dynactin is built around a filament containing eight copies of the actin-related
protein Arp1 and one of β-actin. The filament is capped at each end by distinct
protein complexes, and its length is defined by elongated peptides that emerge
from the α-helical shoulder domain. A further 8.2 angstrom structure of the
complex between dynein, dynactin, and the motility-inducing cargo adaptor
Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that
of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and
dynactin to stabilize the mutually dependent interactions between all three
components.
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