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

SASDNS8 – High mannose contactin-2 immunoglobulin domains1-6, 13μM

Contactin-2
MWI(0) 167 kDa
MWexpected 150 kDa
VPorod 350 nm3
log I(s) 1.23×10-1 1.23×10-2 1.23×10-3 1.23×10-4
Contactin-2 small angle scattering data  s, nm-1
ln I(s)
Contactin-2 Guinier plot ln 1.24×10-1 Rg: 5.5 nm 0 (5.5 nm)-2 s2
(sRg)2I(s)/I(0)
Contactin-2 Kratky plot 1.104 0 3 sRg
Dmax: 21.4 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of High mannose contactin-2 immunoglobulin domains1-6, 13μM in 25 mM HEPES, 150 mM NaCl, 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 0.97 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 7 N-glycosylation sites confirmed crystallographically.

Contactin-2
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   75.2 kDa
 
UniProt   Q61330 (29-608)
Sequence   FASTA