Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation.

Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C, Matrix Biol (2022) Europe PMC

SASDNR3 – Fibrillin-1 fragment PF3

Fibrillin-1 PF3
MWexperimental 86 kDa
MWexpected 78 kDa
VPorod 141 nm3
log I(s) 1.08×102 1.08×101 1.08×100 1.08×10-1
Fibrillin-1 PF3 small angle scattering data  s, nm-1
ln I(s)
Fibrillin-1 PF3 Guinier plot ln 1.08×102 Rg: 5.4 nm 0 (5.4 nm)-2 s2
(sRg)2I(s)/I(0)
Fibrillin-1 PF3 Kratky plot 1.104 0 √3 sRg
p(r)
Fibrillin-1 PF3 pair distance distribution function Rg: 5.7 nm 0 Dmax: 24 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fibrillin-1 PF3 DAMMIF model
Synchrotron SAXS data from solutions of Fibrillin-1 fragment PF3 in Tris buffered saline, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.1 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 50.00 μl sample at 5 mg/ml was injected at a 0.05 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column. 2000 successive 1 second frames were collected where SAXS data frames 1421 - 1457 were used for processing. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Fibrillin-1 PF3 (Fbn1 pf3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   77.7 kDa
 
UniProt   P35555 (1-722)
Sequence   FASTA