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- SASDBU2: Human Arpin (isoform 1) (Human Arpin) -

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Basic information

Entry
Database: SASBDB / ID: SASDBU2
SampleHuman Arpin (isoform 1)
  • Human Arpin (protein), Human Arpin, Homo sapiens
Function / homologyArpin / Arp2/3-interacting proteins Arpin / negative regulation of lamellipodium morphogenesis / negative regulation of actin nucleation / directional locomotion / negative regulation of cell migration / lamellipodium / Arpin
Function and homology information
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: Human Arpin (isoform 1)
BufferName: 50 mM HEPES 100mM NaCl 1mM TCEP / Concentration: 50.00 mM / pH: 7.5 / Composition: 100mM NaCl, 1mM TCEP
Entity #275Name: Human Arpin / Type: protein / Description: Human Arpin / Formula weight: 24.869 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q7Z6K5
Sequence: GSRIYHDGAL RNKAVQSVRL PGAWDPAAHQ GGNGVLLEGE LIDVSRHSIL DTHGRKERYY VLYIRPSHIH RRKFDAKGNE IEPNFSATRK VNTGFLMSSY KVEAKGDTDR LTPEALKGLV NKPELLALTE SLTPDHTVAF WMPESEMEVM ELELGAGVRL KTRGDGPFLD ...Sequence:
GSRIYHDGAL RNKAVQSVRL PGAWDPAAHQ GGNGVLLEGE LIDVSRHSIL DTHGRKERYY VLYIRPSHIH RRKFDAKGNE IEPNFSATRK VNTGFLMSSY KVEAKGDTDR LTPEALKGLV NKPELLALTE SLTPDHTVAF WMPESEMEVM ELELGAGVRL KTRGDGPFLD SLAKLEAGTV TKCNFTGDGK TGASWTDNIM AQKCSKGAAA EIREQGDGAE DEEWDD

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Experimental information

BeamInstrument name: SOLEIL SWING / City: Saint-Aubin / : France / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 1.82 mm
DetectorName: AVIEX PCCD170170 / Type: CCD
Scan
Title: Human Arpin (isoform 1) / Measurement date: Dec 4, 2014 / Storage temperature: 15 °C / Cell 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: 791 /
MinMax
Q0.112661 4.5532
P(R) point1 791
R0 13.2
Result
Type of curve: single_conc
Comments: Due to high concentration at the elution peak, the HPLC UV detector was saturated and the concentrations of the sample was consequently underestimated. In this case, the molecular mass is ...Comments: Due to high concentration at the elution peak, the HPLC UV detector was saturated and the concentrations of the sample was consequently underestimated. In this case, the molecular mass is overestimated when assessing this parameter from I(0) and concentration.
ExperimentalStandardPorod
MW27.4 kDa27.4 kDa27.8 kDa
Volume--47.23 nm3

P(R)GuinierP(R) error
Forward scattering, I00.05 0.05 -
Radius of gyration, Rg2.77 nm2.6 nm0.05

MinMax
D-13.2
Guinier point10 82

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