Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions

Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B, The EMBO Journal (2022) DOI

SASDKX4 – Teneurin-4 dimer mutant in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA)

Teneurin-4 (S2585C)
MWexperimental 600 kDa
MWexpected 537 kDa
VPorod 1390 nm3
log I(s) 4.60×10-1 4.60×10-2 4.60×10-3 4.60×10-4
Teneurin-4 (S2585C) small angle scattering data  s, nm-1
ln I(s)
Teneurin-4 (S2585C) Guinier plot ln 4.60×10-1 Rg: 7.8 nm 0 (7.8 nm)-2 s2
(sRg)2I(s)/I(0)
Teneurin-4 (S2585C) Kratky plot 1.104 0 √3 sRg
p(r)
Teneurin-4 (S2585C) pair distance distribution function Rg: 8.3 nm 0 Dmax: 31 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Teneurin-4 dimer mutant in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA) Rg histogram Rg, nm
Synchrotron SAXS data from solutions of mutant Teneurin-4 (S2585C) in 20 mM HEPES, 150 mM NaCl, 2 mM EDTA, pH 7.8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.5 m and (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 25 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.

X-ray wavelength: UNKNOWN

Teneurin-4 (S2585C) (TENM4 S2585C)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   268.4 kDa
 
UniProt   Q6N022 (373-2769)
Sequence   FASTA