A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.

Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ, J Biol Chem 299(2):102799 (2023) Europe PMC

SASDRY2 – [(Pro-Pro-Gly)10]3

[(Pro-Pro-Gly)10]3
MWexperimental 8 kDa
MWexpected 8 kDa
VPorod 9 nm3
log I(s) 6.34×10-3 6.34×10-4 6.34×10-5 6.34×10-6
[(Pro-Pro-Gly)10]3 small angle scattering data  s, nm-1
ln I(s)
[(Pro-Pro-Gly)10]3 Guinier plot ln 6.35×10-3 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
[(Pro-Pro-Gly)10]3 Kratky plot 1.104 0 √3 sRg
p(r)
[(Pro-Pro-Gly)10]3 pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
[(Pro-Pro-Gly)10]3 PYMOL model
Synchrotron SAXS data from solutions of (PPG)10 in 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL, pH 6 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 20°C. 60 successive 1 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.

[(Pro-Pro-Gly)10]3 ((PPG)10)
Mol. type   Protein
Organism   synthetic construct
Olig. state   Trimer
Mon. MW   2.5 kDa
Sequence   FASTA