The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode.

Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL, PLoS One 7(8):e41731 (2012) Europe PMC

SASDHZ2 – 14-3-3 protein beta isoform

14-3-3 protein beta/alpha
MWI(0) 55 kDa
MWexpected 58 kDa
VPorod 92 nm3
log I(s) 5.87×10-2 5.87×10-3 5.87×10-4 5.87×10-5
14-3-3 protein beta/alpha small angle scattering data  s, nm-1
ln I(s)
14-3-3 protein beta/alpha Guinier plot ln 5.87×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
14-3-3 protein beta/alpha Kratky plot 1.104 0 √3 sRg
p(r)
14-3-3 protein beta/alpha pair distance distribution function Rg: 3.1 nm 0 Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
14-3-3 protein beta/alpha BUNCH model
X-ray synchrotron radiation scattering data from the from the beta isoform of the 14-3-3 protein in 25 mM HEPES 150mM NaCl pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.10332 nm). For both the sample and buffer, five successive 2 second frames were collected from ~80 µl of protein flowed past the beam, where the protein concentration was 1.5 mg/ml. The data were normalized to the intensity of the transmitted beam, place on an absolute scale against water, radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits are from a model optimised using BUNCH. Of note, the intensity error estimates are given as 2-standard errors, thus, the Chi values are a factor of two times lower in the log files than is actually the case.

14-3-3 protein beta/alpha (14-3-3 beta)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   29.1 kDa
 
UniProt   P31946 (1-246)
Sequence   FASTA
 
PDB ID   2BQ0