Contactin 2 homophilic adhesion structure and conformational plasticity

Chataigner L, Thärichen L, Beugelink J, Granneman J, Mokiem N, Snijder J, Förster F, Janssen B, Structure (2023) DOI

SASDN89 – Complex glycan contactin-2 ectodomain, 23 μM

Contactin-2
MWI(0) 406 kDa
MWexpected 389 kDa
VPorod 2044 nm3
log I(s) 7.95×10-1 7.95×10-2 7.95×10-3 7.95×10-4
Contactin-2 small angle scattering data  s, nm-1
ln I(s)
Contactin-2 Guinier plot ln 7.96×10-1 Rg: 12.5 nm 0 (12.5 nm)-2 s2
(sRg)2I(s)/I(0)
Contactin-2 Kratky plot 1.104 0 3 sRg
Dmax: 65 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Complex glycan contactin-2 ectodomain, 23 μM in 25 mM HEPES, 500 mM NaCl, 500 mM imidazole, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.03 mg/ml was measured at 21°C. 15 successive 0.100 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.

Total expected molecular weight = Amino acid sequence MW + MW for 11 predicted N-glycosylation sites.

Contactin-2
Mol. type   Protein
Organism   Mus musculus
Olig. state   Trimer
Mon. MW   129.8 kDa
 
UniProt   Q61330 (29-1004)
Sequence   FASTA