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

SASDB55 – Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

Myelin-associated glycoprotein Ig domains 1-5
MWexperimental 77 kDa
MWexpected 108 kDa
VPorod 177 nm3
log I(s) 7.67×101 7.67×100 7.67×10-1 7.67×10-2
Myelin-associated glycoprotein Ig domains 1-5 small angle scattering data  s, nm-1
ln I(s)
Myelin-associated glycoprotein Ig domains 1-5 Guinier plot ln 7.68×101 Rg: 6.8 nm 0 (6.8 nm)-2 s2
(sRg)2I(s)/I(0)
Myelin-associated glycoprotein Ig domains 1-5 Kratky plot 1.104 0 √3 sRg
p(r)
Myelin-associated glycoprotein Ig domains 1-5 pair distance distribution function Rg: 7.0 nm 0 Dmax: 23.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myelin-associated glycoprotein Ig domains 1-5 NONE model
Myelin-associated glycoprotein Ig domains 1-5 NONE model
X-ray synchrotron radiation scattering data from solutions of myelin-associated glycoprotein in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle). One solute concentration of 3.38 mg/ml was measured from nine successive 2 second frames. 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. The low angle data collected were obtained from a single concentration scattering curve.

The model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.

Myelin-associated glycoprotein Ig domains 1-5 (MAG)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   54.0 kDa
 
UniProt   P20917 (20-508)
Sequence   FASTA