Structure and RNA interactions of the N-terminal RRM domains of PTB.

Simpson PJ, Monie TP, Szendröi A, Davydova N, Tyzack JK, Conte MR, Read CM, Cary PD, Svergun DI, Konarev PV, Curry S, Matthews S, Structure 12(9):1631-43 (2004) Europe PMC

SASDM77 – Full-length polypyrimidine tract binding protein (PTB)

Polypyrimidine tract-binding protein 2
MWexperimental 60 kDa
MWexpected 57 kDa
VPorod 117 nm3
log I(s) 2.05×102 2.05×101 2.05×100 2.05×10-1
Polypyrimidine tract-binding protein 2 small angle scattering data  s, nm-1
ln I(s)
Polypyrimidine tract-binding protein 2 Guinier plot ln 2.06×102 Rg: 4.0 nm 0 (4.0 nm)-2 s2
(sRg)2I(s)/I(0)
Polypyrimidine tract-binding protein 2 Kratky plot 1.104 0 √3 sRg
p(r)
Polypyrimidine tract-binding protein 2 pair distance distribution function Rg: 4.2 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Polypyrimidine tract-binding protein 2 DAMMIN model
Synchrotron SAXS data from solutions of Full-length polypyrimidine tract binding protein (PTB) in 25 mM Tris, 250 mM NaCl, 2 mM DTT, pH 7.2 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a 1D Gas detector detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 3.4 and 20 mg/ml were measured at 25°C. 12 successive 60 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Tags: X33
Polypyrimidine tract-binding protein 2 (PTB)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   57.5 kDa
 
UniProt   Q9UKA9 (1-531)
Sequence   FASTA