Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states

Stachowski T, Snell M, Snell E, IUCrJ 7(2) (2020) DOI

SASDG55 – Deglycosylated latency associated peptide, LAP (TGFB-1)

Latency associated peptide
MWI(0) 47 kDa
MWexpected 58 kDa
VPorod 129 nm3
log I(s) 1.99×100 1.99×10-1 1.99×10-2 1.99×10-3
Latency associated peptide small angle scattering data  s, nm-1
ln I(s)
Latency associated peptide Guinier plot ln 1.99×100 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Latency associated peptide Kratky plot 1.104 0 √3 sRg
p(r)
Latency associated peptide pair distance distribution function Rg: 3.6 nm 0 Dmax: 13 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of deglycosylated latency associated peptide (LAP) from the transforming growth factor beta-1 proprotein (TGFB-1) in phosphate buffered saline, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.40 mg/ml was measured at 10°C. 100 successive 0.100 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.

Latency associated peptide (LAP)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   29.2 kDa
 
UniProt   P01137 (30-277)
Sequence   FASTA