A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR).

Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M, J Biol Chem 287(41):34304-15 (2012) Europe PMC

SASDAU4 – uPAR H47C/N259C

Urokinase plasminogen activator surface receptor
MWI(0) 34 kDa
MWexpected 37 kDa
VPorod 57 nm3
log I(s) 3.67×101 3.67×100 3.67×10-1 3.67×10-2
Urokinase plasminogen activator surface receptor small angle scattering data  s, nm-1
ln I(s)
Urokinase plasminogen activator surface receptor Guinier plot ln 3.67×101 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Urokinase plasminogen activator surface receptor Kratky plot 1.104 0 √3 sRg
p(r)
Urokinase plasminogen activator surface receptor pair distance distribution function Rg: 2.2 nm 0 Dmax: 7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Urokinase plasminogen activator surface receptor DAMMIF model
log I(s)
 s, nm-1
Urokinase plasminogen activator surface receptor CORAL model
Synchrotron SAXS data from solutions of uPAR H47C/N259C in 25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH 7.2 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 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 1.5 and 4.4 mg/ml were measured at 10°C. Four successive 30 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
Urokinase plasminogen activator surface receptor (uPAR)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   37.0 kDa
 
UniProt   Q03405
Sequence   FASTA