Functional and structural insight into properdin control of complement alternative pathway amplification.

Pedersen DV, Roumenina L, Jensen RK, Gadeberg TA, Marinozzi C, Picard C, Rybkine T, Thiel S, Sørensen UB, Stover C, Fremeaux-Bacchi V, Andersen GR, EMBO J 36(8):1084-1099 (2017) Europe PMC

SASDB69 – E244K monomeric human Properdin

E244K Human Properdin
MWexperimental 50 kDa
MWexpected 49 kDa
log I(s) 1.66×104 1.66×103 1.66×102 1.66×101
E244K Human Properdin small angle scattering data  s, nm-1
ln I(s)
E244K Human Properdin Guinier plot ln 1.67×104 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
E244K Human Properdin Kratky plot 1.104 0 √3 sRg
Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
E244K Human Properdin CORAL model
Synchrotron SAXS data from solutions of recombinantly formed monomeric human E244K properdin in 10 mM HEPES pH 7.2, 150 mM NaCl, were collected EMBL-P12 bioSAXS beam line at the PETRAIII storage ring (Hamburg, Germany) equipped with a Pilatus 2M detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle; λ = 0.124 nm). A solute concentration of 2.7 mg/ml was measured at 20°C. 20 successive 0.05 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 and scaled for protein concentration.

E244K Human Properdin (E244K FP)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   49.3 kDa
 
UniProt   P27918
Sequence   FASTA