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

SASDKB4 – Complement factor P, properdin (FP) trimer

Properdin (trimer)
MWexperimental 135 kDa
MWexpected 165 kDa
log I(s) 2.34×104 2.34×103 2.34×102 2.34×101
Properdin (trimer) small angle scattering data  s, nm-1
ln I(s)
Properdin (trimer) Guinier plot ln 2.35×104 Rg: 10.2 nm 0 (10.2 nm)-2 s2
(sRg)2I(s)/I(0)
Properdin (trimer) Kratky plot 1.104 0 3 sRg
Dmax: 27 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Properdin (trimer) OTHER [STATIC IMAGE] model

Synchrotron SAXS data from solutions of complement factor P, properdin (FP) trimer 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column. 14 successive 1 second frames were collected through the SEC elution peak of the sample. 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 (trimer) (FP trimer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Trimer
Mon. MW   55 kDa
 
UniProt   P27918 (28-469)
Sequence   FASTA