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- SASDBT2: Ankyrin repeat domains from human Tankyrase-2 (489-649) -

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Basic information

Entry
Database: SASBDB / ID: SASDBT2
SampleAnkyrin repeat domains from human Tankyrase-2 (489-649)
  • Ankyrin repeat domains from Tankyrase 2 (protein), Tankyrase-2(489-649), Homo sapiens
Function / homology
Function and homology information


XAV939 stabilizes AXIN / NAD+ ADP-ribosyltransferase / protein localization to chromosome, telomeric region / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein poly-ADP-ribosylation / pericentriolar material / positive regulation of telomere capping / NAD+-protein ADP-ribosyltransferase activity / NAD+ ADP-ribosyltransferase activity ...XAV939 stabilizes AXIN / NAD+ ADP-ribosyltransferase / protein localization to chromosome, telomeric region / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein poly-ADP-ribosylation / pericentriolar material / positive regulation of telomere capping / NAD+-protein ADP-ribosyltransferase activity / NAD+ ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / positive regulation of telomere maintenance via telomerase / nucleotidyltransferase activity / TCF dependent signaling in response to WNT / Degradation of AXIN / Wnt signaling pathway / Regulation of PTEN stability and activity / protein polyubiquitination / positive regulation of canonical Wnt signaling pathway / nuclear envelope / chromosome, telomeric region / Ub-specific processing proteases / Golgi membrane / perinuclear region of cytoplasm / enzyme binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Ankyrin repeat / Ankyrin repeats (many copies) / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily ...Ankyrin repeat / Ankyrin repeats (many copies) / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Ankyrin repeat / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily
Similarity search - Domain/homology
Poly [ADP-ribose] polymerase tankyrase-2
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationJournal: Structure / Year: 2016
Title: Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.
Authors: Susan Fetics / Aurélien Thureau / Valérie Campanacci / Magali Aumont-Nicaise / Irène Dang / Alexis Gautreau / Javier Pérez / Jacqueline Cherfils /
Abstract: 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 ...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.
Contact author
  • Aurélien Thureau (Soleil, Soleil Synchrotron, Saint-Aubin, France)

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Structure visualization

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Models

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Sample

SampleName: Ankyrin repeat domains from human Tankyrase-2 (489-649)
BufferName: 50 mM HEPES 100mM NaCl 1mM TCEP / Concentration: 50.00 mM / pH: 7.5 / Composition: 100mM NaCl, 1mM TCEP
Entity #274Name: Tankyrase-2(489-649) / Type: protein / Description: Ankyrin repeat domains from Tankyrase 2 / Formula weight: 17.565 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q9H2K2
Sequence:
GNSEADRQLL EAAKAGDVET VKKLCTVQSV NCRDIEGRQS TPLHFAAGYN RVSVVEYLLQ HGADVHAKDK GGLVPLHNAC SYGHYEVAEL LVKHGAVVNV ADLWKFTPLH EAAAKGKYEI CKLLLQHGAD PTKKNRDGNT PLDLVKDGDT DIQDLLRGDA AL

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Experimental information

BeamInstrument name: SOLEIL SWING / City: Saint-Aubin / : France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 1.82 mm
DetectorName: AVIEX PCCD170170 / Type: CCD
Scan
Title: Ankyrin repeat domains from human Tankyrase-2 / Measurement date: Dec 4, 2014 / Storage temperature: 15 °C / Exposure time: 1.5 sec. / Unit: 1/nm /
MinMax
Q0.062 6.0833
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 928 /
MinMax
Q0.185891 5.3918
P(R) point1 928
R0 6.25
Result
Type of curve: single_conc
ExperimentalStandardPorod
MW17.1 kDa17.1 kDa15 kDa
Volume--23.6 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.0444 2.0E-5 0.044 3.0E-5
Radius of gyration, Rg1.84 nm0.001 1.77 nm0.01

MinMax
D-6.25
Guinier point23 111

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