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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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PDB id:
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Protein binding
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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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Structure:
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Tankyrase-2. Chain: a. Fragment: ankyrin repeats domain, unp residues 490-644. Synonym: tank2,adp-ribosyltransferase diphtheria toxin-like 6,artd6, poly [adp-ribose] polymerase 5b,tnks-2,trf1-interacting ankyrin- related adp-ribose polymerase 2,tankyrase ii,tankyrase-like protein, tankyrase-related protein. Engineered: yes. Glu-ile-arg-glu-gln-gly-asp-gly-ala-glu-asp-glu.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: tnks2, parp5b, tank2, tnkl. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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1.86Å
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R-factor:
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0.175
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R-free:
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0.217
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Authors:
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S.K.Fetics,V.Campanacci,I.Dang,A.Gautreau,J.Cherfils
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Key ref:
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S.Fetics
et al.
(2016).
Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.
Structure,
24,
252-260.
PubMed id:
DOI:
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Date:
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04-Apr-15
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Release date:
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30-Dec-15
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PROCHECK
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Headers
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References
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Enzyme class 2:
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Chain A:
E.C.2.4.2.-
- ?????
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Enzyme class 3:
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Chain A:
E.C.2.4.2.30
- NAD(+) ADP-ribosyltransferase.
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Pathway:
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Reaction:
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NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D- ribosyl)n+1-acceptor + H+
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NAD(+)
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+
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(ADP-D-ribosyl)n-acceptor
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=
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nicotinamide
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+
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(ADP-D- ribosyl)n+1-acceptor
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Structure
24:252-260
(2016)
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PubMed id:
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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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S.Fetics,
A.Thureau,
V.Campanacci,
M.Aumont-Nicaise,
I.Dang,
A.Gautreau,
J.Pérez,
J.Cherfils.
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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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Links
