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