Conformational Flexibility and Transient Structure of the Proline-Rich Domain in p53.

Berggren A, Bakker M, Fisher H, Skepö M, Biophys J (2026) Europe PMC

SASDY72 – p53 proline-rich domain of Cellular tumor antigen p53 with(P72R) with 10 mM NaCl and neutral pH

Cellular tumor antigen p53 P72R
MWexperimental 5 kDa
MWexpected 4 kDa
log I(s) 3.39×101 3.39×100 3.39×10-1 3.39×10-2
Cellular tumor antigen p53 P72R small angle scattering data  s, nm-1
ln I(s)
Cellular tumor antigen p53 P72R Guinier plot ln 3.39×101 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Cellular tumor antigen p53 P72R Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of p53 proline-rich domain of Cellular tumor antigen p53 with(P72R) with 10 mM NaCl and neutral pH in 20 mM Tris, 10 mM NaCl,, pH 7 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.48 mg/ml was measured at 20°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cellular tumor antigen p53 P72R (p53 P72R)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   3.8 kDa
 
UniProt   P04637 (62-100)
Sequence   FASTA