Properdin oligomers adopt rigid extended conformations supporting function.

Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR, Elife 10 (2021) Europe PMC

SASDKA4 – Complement factor P, properdin (FP) dimer

Properdin (dimer)
MWI(0) 112 kDa
MWexpected 110 kDa
log I(s) 1.60×10-1 1.60×10-2 1.60×10-3 1.60×10-4
Properdin (dimer) small angle scattering data  s, nm-1
ln I(s)
Properdin (dimer) Guinier plot ln 1.61×10-1 Rg: 8.1 nm 0 (8.1 nm)-2 s2
(sRg)2I(s)/I(0)
Properdin (dimer) Kratky plot 1.104 0 √3 sRg
Dmax: 24 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Properdin (dimer) OTHER [STATIC IMAGE] model
Synchrotron SAXS data from solutions of complement factor P, properdin (FP) dimer in 20 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration was measured at 8°C. 40 successive 0.050 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 atomic coordinate file of the model (.pdb format) is made available in the 'Additional' folder of the full entry zip archive.

Properdin (dimer) (FP dimer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   55 kDa
 
UniProt   P27918 (28-469)
Sequence   FASTA