Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition

Gogou C, Beugelink J, Frias C, Kresik L, Jaroszynska N, Drescher U, Janssen B, Hindges R, Meijer D, Nature Communications 15(1) (2024) DOI

SASDTD3 – Teneurin-3 A0B1 isoform in 5 mM EDTA - 0.62 mg/mL

Isoform A0B1 of Teneurin-3
MWI(0) 549 kDa
MWexpected 545 kDa
VPorod 987 nm3
log I(s) 3.37×102 3.37×101 3.37×100 3.37×10-1
Isoform A0B1 of Teneurin-3 small angle scattering data  s, nm-1
ln I(s)
Isoform A0B1 of Teneurin-3 Guinier plot ln 3.38×102 Rg: 8.7 nm 0 (8.7 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform A0B1 of Teneurin-3 Kratky plot 1.104 0 3 sRg
Dmax: 34 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Teneurin-3 A0B1 isoform in 20 mM HEPES, 150 mM NaCl, 5 mM EDTA, pH 7.8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a wavelength of λ = 0.099188 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.62 mg/ml was 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.

Sample detector distance = UNKNOWN

Isoform A0B1 of Teneurin-3 (Ten3-A0B1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   272.6 kDa
 
UniProt   Q9WTS6-3 (343-2706)
Sequence   FASTA