Structural basis of myelin-associated glycoprotein adhesion and signalling.

Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ, Nat Commun 7:13584 (2016) Europe PMC

SASDB56 – Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) I473E mutant

Myelin-associated glycoprotein (20-508; I473E mutant)
MWI(0) 61 kDa
MWexpected 54 kDa
VPorod 100 nm3
log I(s) 6.11×101 6.11×100 6.11×10-1 6.11×10-2
Myelin-associated glycoprotein (20-508; I473E mutant) small angle scattering data  s, nm-1
ln I(s)
Myelin-associated glycoprotein (20-508; I473E mutant) Guinier plot ln 6.11×101 Rg: 6 nm 0 (6 nm)-2 s2
(sRg)2I(s)/I(0)
Myelin-associated glycoprotein (20-508; I473E mutant) Kratky plot 1.104 0 √3 sRg
p(r)
Myelin-associated glycoprotein (20-508; I473E mutant) pair distance distribution function Rg: 6.3 nm 0 Dmax: 21.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myelin-associated glycoprotein (20-508; I473E mutant) PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of deglycosylated myelin-associated glycoprotein (full extracellular domain (Ig 1-5) I473E mutant) in HEPES, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 2.69 mg/ml was measured at 20°C. 10 successive 2 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 and the different curves were scaled for protein concentration.

Endo-Hf-deglycosylated full extracellular domain of Myelin-associated glycoprotein (MAG) immunoglobulin domains 1-5

Myelin-associated glycoprotein (20-508; I473E mutant) (MAG)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   54.0 kDa
 
UniProt   P20917 (20-508)
Sequence   FASTA
 
PDB ID   5LF5