The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity.

Elena-Real CA, Sagar A, Urbanek A, Popovic M, Morató A, Estaña A, Fournet A, Doucet C, Lund XL, Shi ZD, Costa L, Thureau A, Allemand F, Swenson RE, Milhiet PE, Crehuet R, Barducci A, Cortés J, Sinnaeve D, Sibille N, Bernadó P, Nat Struct Mol Biol (2023) Europe PMC

SASDQR8 – Exon1 of Non pathogenic form of Huntingtin (H16) with GFP fused at the C-terminus

Huntingtin
MWexperimental 39 kDa
MWexpected 39 kDa
VPorod 63 nm3
log I(s) 2.34×10-2 2.34×10-3 2.34×10-4 2.34×10-5
Huntingtin small angle scattering data  s, nm-1
ln I(s)
Huntingtin Guinier plot ln 2.35×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Huntingtin Kratky plot 1.104 0 √3 sRg
Dmax: 16 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Huntingtin OTHER [STATIC IMAGE] model
Synchrotron SAXS data from solutions of Exon1 of the non pathogenic form of Huntingtin (H16) with GFP fused at the C-terminus in 20mM BisTris-HCl, 150mM NaCl, pH 6.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 8 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 10°C. 2100 successive 0.990 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.

Https://proteinensemble.org/entries/PED00223

Tags: PED
Huntingtin (H16)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   39.1 kDa
 
UniProt   P42858 (1-88)
Sequence   FASTA
 
PED ID   PED00223