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PDBsum entry 4z68
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Protein binding
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PDB id
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4z68
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References listed in PDB file
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Key reference
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Title
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Hybrid structural analysis of the arp2/3 regulator arpin identifies its acidic tail as a primary binding epitope.
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Authors
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S.Fetics,
A.Thureau,
V.Campanacci,
M.Aumont-Nicaise,
I.Dang,
A.Gautreau,
J.Pérez,
J.Cherfils.
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Ref.
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Structure, 2016,
24,
252-260.
[DOI no: ]
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PubMed id
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Abstract
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Arpin is a newly discovered regulator of actin polymerization at the cell
leading edge, which steers cell migration by exerting a negative control on the
Arp2/3 complex. Arpin proteins have an acidic tail homologous to the acidic
motif of the VCA domain of nucleation-promoting factors (NPFs). This tail is
predicted to compete with the VCA of NPFs for binding to the Arp2/3 complex,
thereby mitigating activation and/or tethering of the complex to sites of actin
branching. Here, we investigated the structure of full-length Arpin using
synchrotron small-angle X-ray scattering, and of its acidic tail in complex with
an ankyrin repeats domain using X-ray crystallography. The data were combined in
a hybrid model in which the acidic tail extends from the globular core as a
linear peptide and forms a primary epitope that is readily accessible in unbound
Arpin and suffices to tether Arpin to interacting proteins with high affinity.
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