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PDBsum entry 4n78
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Protein binding
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PDB id
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4n78
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Contents |
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1184 a.a.
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1085 a.a.
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202 a.a.
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67 a.a.
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156 a.a.
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PDB id:
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| Name: |
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Protein binding
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Title:
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The wave regulatory complex links diverse receptors to the actin cytoskeleton
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Structure:
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Cytoplasmic fmr1-interacting protein 1. Chain: a. Synonym: specifically rac1-associated protein 1, sra-1, p140sra-1. Engineered: yes. Nck-associated protein 1. Chain: b. Synonym: nap 1, membrane-associated protein hem-2, p125nap1. Engineered: yes. Wiskott-aldrich syndrome protein family member 1.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cyfip1, kiaa0068. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: nckap1, hem2, kiaa0587, nap1. Gene: wasf1, kiaa0269, scar1, wave1. Expressed in: escherichia coli.
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Resolution:
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2.43Å
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R-factor:
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0.189
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R-free:
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0.209
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Authors:
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Z.C.Chen
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Key ref:
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B.Chen
et al.
(2014).
The WAVE regulatory complex links diverse receptors to the actin cytoskeleton.
Cell,
156,
195-207.
PubMed id:
DOI:
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Date:
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15-Oct-13
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Release date:
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05-Feb-14
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PROCHECK
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Headers
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References
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Q7L576
(CYFP1_HUMAN) -
Cytoplasmic FMR1-interacting protein 1 from Homo sapiens
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Seq: Struc:
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1253 a.a.
1184 a.a.
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Q9Y2A7
(NCKP1_HUMAN) -
Nck-associated protein 1 from Homo sapiens
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Seq: Struc:
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1128 a.a.
1085 a.a.
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Q92558
(WASF1_HUMAN) -
Actin-binding protein WASF1 from Homo sapiens
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Seq: Struc:
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559 a.a.
202 a.a.*
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DOI no:
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Cell
156:195-207
(2014)
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PubMed id:
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The WAVE regulatory complex links diverse receptors to the actin cytoskeleton.
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B.Chen,
K.Brinkmann,
Z.Chen,
C.W.Pak,
Y.Liao,
S.Shi,
L.Henry,
N.V.Grishin,
S.Bogdan,
M.K.Rosen.
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ABSTRACT
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The WAVE regulatory complex (WRC) controls actin cytoskeletal dynamics
throughout the cell by stimulating the actin-nucleating activity of the Arp2/3
complex at distinct membrane sites. However, the factors that recruit the WRC to
specific locations remain poorly understood. Here, we have identified a large
family of potential WRC ligands, consisting of ∼120 diverse membrane proteins,
including protocadherins, ROBOs, netrin receptors, neuroligins, GPCRs, and
channels. Structural, biochemical, and cellular studies reveal that a sequence
motif that defines these ligands binds to a highly conserved interaction surface
of the WRC formed by the Sra and Abi subunits. Mutating this binding surface in
flies resulted in defects in actin cytoskeletal organization and egg morphology
during oogenesis, leading to female sterility. Our findings directly link
diverse membrane proteins to the WRC and actin cytoskeleton and have broad
physiological and pathological ramifications in metazoans.
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');
}
}
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