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) Europe PMC

SASDB63 – Human dystrophin central domain repeats 11 to 15

Dystrophin central domain repeats 11 to 15.
MWexperimental 54 kDa
MWexpected 60 kDa
VPorod 87 nm3
log I(s) 1.01×101 1.01×100 1.01×10-1 1.01×10-2
Dystrophin central domain repeats 11 to 15. small angle scattering data  s, nm-1
ln I(s)
Dystrophin central domain repeats 11 to 15. Guinier plot ln 1.02×101 Rg: 5.8 nm 0 (5.8 nm)-2 s2
(sRg)2I(s)/I(0)
Dystrophin central domain repeats 11 to 15. Kratky plot 1.104 0 √3 sRg
p(r)
Dystrophin central domain repeats 11 to 15. pair distance distribution function Rg: 6.0 nm 0 Dmax: 23 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Dystrophin central domain repeats 11 to 15. NONE model
Synchrotron SAXS data were measured from solutions of Human Dystrophin central domain repeats 11 to 15 (amino acids 1461-1973) in 20 mM Tris 150 mM NaCl, 1 mM EDTA, 2% glycerol using a series of 5 concentrations (1.1, 2.1, 4.6, 6.4 and 10.8 mg/ml) and injected into the SAXS capillary using an automatic liquid dispensing robot (sample changer at ID14-eh3 of the ESRF, Grenoble (France). Ten frames of 1.5 seconds each were collected for the buffer (TNE) and the R11-15 protein samples at different concentrations; after buffer subtraction, frames were then averaged after visual inspection. The molecular weight estimates (MW) are derived from the Porod volume, Vp, where MW is approximately Vp/1.6.

Cell temperature = UNKNOWN

Dystrophin central domain repeats 11 to 15. (Dystrophin 1461-1973)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   60.1 kDa
 
UniProt   P11532 (1461-1973)
Sequence   FASTA