Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.

Haataja TJK, Bernardi RC, Lecointe S, Capoulade R, Merot J, Pentikäinen U, Structure (2018) Europe PMC

SASDEQ7 – Filamin A Ig-like domains 3-5 (FLNa3-5)

Filamin A Ig-like domains 3-5
MWexperimental 25 kDa
MWexpected 31 kDa
VPorod 39 nm3
log I(s) 2.56×101 2.56×100 2.56×10-1 2.56×10-2
Filamin A Ig-like domains 3-5 small angle scattering data  s, nm-1
ln I(s)
Filamin A Ig-like domains 3-5 Guinier plot ln 2.56×101 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Filamin A Ig-like domains 3-5 Kratky plot 1.104 0 √3 sRg
p(r)
Filamin A Ig-like domains 3-5 pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Filamin A Ig-like domains 3-5 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Filamin A Ig-like domains 3-5 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 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.

SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).

Filamin A Ig-like domains 3-5 (FLNa3-5)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   30.8 kDa
 
UniProt   P21333 (478-766)
Sequence   FASTA
 
PDB ID   4M9P