Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.

Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E, J Biol Chem 293(18):6637-6646 (2018) PubMed

SASDBV3 – Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47)
MWexperimental 210 kDa
MWexpected 64 kDa
VPorod 184 nm3
log I(s) 1.04×10-4 1.04×10-5 1.04×10-6 1.04×10-7
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) small angle scattering data  s, nm-1
ln I(s)
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) Guinier plot ln 1.05×10-4 Rg: 6.0 nm 0 (6.0 nm)-2 s2
(sRg)2I(s)/I(0)
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) Kratky plot 1.104 0 3 sRg
p(r)
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) pair distance distribution function Rg: 6.0 nm 0 Dmax: 21 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) GASBOR model

Synchrotron SAXS data were measured from solutions of Human Dystrophin central domain repeats 16 to 21 Becker muscular dystrophy variant (Δ2146-2305 deletion of exons 45-47) in 20 mM Tris 150 mM NaCl, 1 mM EDTA, 2% glycerol, 5% acetonitrile buffer using size exclusion chromatography (SEC-SAXS) on the SWING beam line (SOLEIL, Saint-Aubin, France). The sample load concentration was 5 mg/mL. The scattering data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected through the corresponding SEC protein elution peak (21 x 1.5 s frames) as well as from the SEC column running buffer. The buffer scattering contributions were subtracted from each sample frame, which were then scaled and averaged to produce the SAXS profile displayed in this entry. The corresponding UV SEC-SAXS trace can be found in the full entry zip archive. The SAXS acquisition was performed on the peak positioned at 11.49 minutes on the 280 nm UV trace where the SEC-SAXS frames produced consistent Rg and I(0). The experimental MW was estimated from exclusion chromatography to be 210 kDa for a Stokes radius of 6.3 nm. However, as the protein is elongated, the calculation of the MW from Stokes radius is a large overestimation. In addition to the the Gasbor model displayed above, an image of the protein viewed as a continuous volume representation is also included in the full entry zip archive following the protocol designed by John Stone et al. (VMD, MDFF package).

Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) (Dystrophin1991-2694Δ)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   63.9 kDa
 
UniProt   P11532 (1991-2694)
Sequence   FASTA