Structural insights into the contactin 1 – neurofascin 155 adhesion complex

Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B, Nature Communications 13(1) (2022) DOI

SASDLQ6 – High mannose glycan contactin 1 immunoglobulin domains 1-6, 2.7 μM

Contactin-1 I433V
MWI(0) 89 kDa
MWexpected 134 kDa
VPorod 100 nm3
log I(s) 1.15×10-2 1.15×10-3 1.15×10-4 1.15×10-5
Contactin-1 I433V small angle scattering data  s, nm-1
ln I(s)
Contactin-1 I433V Guinier plot ln 1.15×10-2 Rg: 4.9 nm 0 (4.9 nm)-2 s2
(sRg)2I(s)/I(0)
Contactin-1 I433V Kratky plot 1.104 0 √3 sRg
p(r)
Contactin-1 I433V pair distance distribution function Rg: 4.8 nm 0 Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Contactin-1 I433V CUSTOM IN-HOUSE model
Synchrotron SAXS data from solutions of High mannose glycan contactin 1 immunoglobulin domains 1-6, 2.7 μM 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 (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.18 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

High mannose glycan contactin 1 immunoglobulin domains 1-6 2.7μM. Experimental molecular weight=Sequence Expected MW + MW for 6 N glycosylation sites confirmed crystallographically. X-ray wavelength: UNKNOWN. X-ray exposure time: UNKNOWN. Experimental temperature: UNKNOWN. Dmax underestimated.

Contactin-1 I433V
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   66.8 kDa
 
UniProt   P12960 (21-604)
Sequence   FASTA