Skeletal Dysplasia Mutations Effect on Human Filamins' Structure and Mechanosensing.

Seppälä J Bernardi RC, Haataja TJK, Hellman M, Pentikäinen OT, Schulten K, Permi P, Ylänne J, Pentikäinen U, Sci Rep 7(1):4218 (2017) Europe PMC

SASDB32 – Human Filamin A Ig-like domains 16-17 truncation (1782-1956)

Human Filamin A Ig-like domains 16-17
MWI(0) 20 kDa
MWexpected 19 kDa
VPorod 31 nm3
log I(s) 3.03×101 3.03×100 3.03×10-1 3.03×10-2
Human Filamin A Ig-like domains 16-17 small angle scattering data  s, nm-1
ln I(s)
Human Filamin A Ig-like domains 16-17 Guinier plot ln 3.03×101 Rg: 1.8 nm 0 (1.8 nm)-2 s2
(sRg)2I(s)/I(0)
Human Filamin A Ig-like domains 16-17 Kratky plot 1.104 0 √3 sRg
p(r)
Human Filamin A Ig-like domains 16-17 pair distance distribution function Rg: 1.8 nm 0 Dmax: 6.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Human Filamin A Ig-like domains 16-17 DAMMIN model
Synchrotron SAXS data from solutions of Human Filamin A Ig-like domains 16-17 truncation (1782-1956) in 20 mM Tris 50 mM NaCl 10 mM DTT were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.093 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 5 mg/ml were 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Human Filamin A Ig-like domains 16-17 (FilaminA)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   18.7 kDa
 
UniProt   P21333 (1782-1956)
Sequence   FASTA