Characterizing two nanobodies for SMAD4.

Condeminas M Torner C, Pluta R, Ruiz L, R de Régil M, Khan RJ, Pous J, Pardon E, Steyaert J, Fromm S, Martin-Malpartida P, Macias MJ, FEBS Lett (2026) Europe PMC

SASDWQ9 – Mothers against decapentaplegic homolog 4 (SMAD4) C-terminal domain (amino acids 272-552, S4SADMH2)

Mothers against decapentaplegic homolog 4
MWexperimental 33 kDa
MWexpected 31 kDa
VPorod 45 nm3
log I(s) 4.30×101 4.30×100 4.30×10-1 4.30×10-2
Mothers against decapentaplegic homolog 4 small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 4 Guinier plot ln 4.30×101 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 4 Kratky plot 1.104 0 √3 sRg
p(r)
Mothers against decapentaplegic homolog 4 pair distance distribution function Rg: 2.5 nm 0 Dmax: 9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the SMAD4 C-terminal domain in 20 mM TRIS, 200 mM NaCl, 1 mM DTT, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.32 mg/ml was measured at 20°C. 10 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.

Mothers against decapentaplegic homolog 4 (SMAD4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   31.2 kDa
 
UniProt   Q13485 (272-552)
Sequence   FASTA