Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly.

Lockhart-Cairns MP, Newandee H, Thomson J, Weiss AS, Baldock C, Tarakanova A, J Mol Biol 432(21):5736-5751 (2020) Europe PMC

SASDNU3 – Fibrillin PF2

Fibrillin-1
MWexperimental 43 kDa
MWexpected 44 kDa
VPorod 84 nm3
log I(s) 4.36×10-2 4.36×10-3 4.36×10-4 4.36×10-5
Fibrillin-1 small angle scattering data  s, nm-1
ln I(s)
Fibrillin-1 Guinier plot ln 4.36×10-2 Rg: 4.3 nm 0 (4.3 nm)-2 s2
(sRg)2I(s)/I(0)
Fibrillin-1 Kratky plot 1.104 0 √3 sRg
p(r)
Fibrillin-1 pair distance distribution function Rg: 4.6 nm 0 Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fibrillin-1 DAMMIF model
log I(s)
 s, nm-1
Fibrillin-1 OTHER model
Fibrillin-1 BILBOMD model
Fibrillin-1 BILBOMD model
Synchrotron SAXS data from solutions of fibrillin PF2 in Tris buffered saline, pH 7.4 were collected on the ID02 beam line at the ESRF (Grenoble, France) and merged with data from the B21 beam line of the Diamond Light Source (Didcot, UK). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

PF2 data first presented in the 2006 paper "Nanostructure of fibrillin-1 reveals compact conformation of EGF arrays and mechanism for extensibility" (Baldock et al. 2006).

Fibrillin-1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   44.2 kDa
 
UniProt   P35555 (330-722)
Sequence   FASTA