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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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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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PDB id:
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| Name: |
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Motor protein
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Title:
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Cryo-em structure of dynein tail-dynactin-bicd2n complex
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Structure:
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Dynein tail. Chain: 1. Dynein tail. Chain: 2. Dynein tail. Chain: 3, 4. Dynein tail. Chain: 5, 6. Dynactin.
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Source:
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Sus scrofa. Pig. Organism_taxid: 9823. Organ: brain. Organ: brain
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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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Key ref:
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L.Urnavicius
et al.
(2015).
The structure of the dynactin complex and its interaction with dynein.
Science,
347,
1441-1446.
PubMed id:
DOI:
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Date:
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26-Jan-15
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Release date:
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11-Mar-15
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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A0A0J9X2A1
(A0A0J9X2A1_PIG) -
Dynein tail from Sus scrofa
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Seq: Struc:
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350 a.a.
350 a.a.
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No UniProt id for this chain
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F2Z5G5
(F2Z5G5_PIG) -
Alpha-centractin from Sus scrofa
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Seq: Struc:
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349 a.a.
370 a.a.*
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Q6QAQ1
(ACTB_PIG) -
Actin, cytoplasmic 1 from Sus scrofa
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Seq: Struc:
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375 a.a.
370 a.a.
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I3LHK5
(I3LHK5_PIG) -
Actin-related protein 10 from Sus scrofa
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Seq: Struc:
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417 a.a.
369 a.a.
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A0PFK5
(A0PFK5_PIG) -
F-actin-capping protein subunit alpha-1 from Sus scrofa
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Seq: Struc:
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286 a.a.
275 a.a.
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D2JYW4
(D2JYW4_PIG) -
F-actin-capping protein subunit beta from Sus scrofa
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Seq: Struc:
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277 a.a.
270 a.a.
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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D0G6S1
(D0G6S1_PIG) -
Dynactin subunit 6 from Sus scrofa
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Seq: Struc:
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190 a.a.
168 a.a.*
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A0A286ZK88
(A0A286ZK88_PIG) -
Dynactin subunit 5 from Sus scrofa
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Seq: Struc:
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182 a.a.
165 a.a.*
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No UniProt id for this chain
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No UniProt id for this chain
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A0A0J9X292
(A0A0J9X292_PIG) -
Dynactin from Sus scrofa
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Seq: Struc:
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48 a.a.
48 a.a.
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A0A0J9X293
(A0A0J9X293_PIG) -
Dynactin subunit 2 from Sus scrofa
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Seq: Struc:
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71 a.a.
71 a.a.
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DOI no:
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Science
347:1441-1446
(2015)
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PubMed id:
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The structure of the dynactin complex and its interaction with dynein.
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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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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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');
}
}
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