Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.

Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J, Structure 24(2):252-60 (2016) Europe PMC

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

Ankyrin repeat domains from Tankyrase 2
MWI(0) 17 kDa
MWexpected 18 kDa
VPorod 24 nm3
log I(s) 4.40×10-2 4.40×10-3 4.40×10-4 4.40×10-5
Ankyrin repeat domains from Tankyrase 2 small angle scattering data  s, nm-1
ln I(s)
Ankyrin repeat domains from Tankyrase 2 Guinier plot ln 4.40×10-2 Rg: 1.8 nm 0 (1.8 nm)-2 s2
(sRg)2I(s)/I(0)
Ankyrin repeat domains from Tankyrase 2 Kratky plot 1.104 0 √3 sRg
p(r)
Ankyrin repeat domains from Tankyrase 2 pair distance distribution function Rg: 1.8 nm 0 Dmax: 6.3 nm

Data validation

There are no models related to this curve.

X-ray synchrotron radiation scattering data from solutions of the Ankyrin repeat domains from human Tankyrase-2 (amino acids 489-649) in 50mM HEPES, pH 7.5, 100mM NaCl, 1mM TCEP were collected at 15 C on the SWING Beamline, Synchrotron Soleil, Gif Sur Yvette, France using a PCCD170170 Aviex detector. These data are derived from size-exclusion chromatography-SAXS. Note: The original SAXS data where the momentum transfer s in inverse Angstroms (s = 4π sin θ/λ, where 2θ is the scattering angle) is included in the zip file associated with this entry.

Cell temperature = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN

Ankyrin repeat domains from Tankyrase 2 (Tankyrase-2(489-649))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   17.6 kDa
 
UniProt   Q9H2K2 (489-649)
Sequence   FASTA