The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue.

Finci LI, Kr├╝ger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R, Neuron 83(4):839-849 (2014) Europe PMC


MWexperimental 48 kDa
MWexpected 49 kDa
VPorod 100 nm3
log I(s) 3.63×103 3.63×102 3.63×101 3.63×100
Netrin-1 small angle scattering data  s, nm-1
ln I(s)
Netrin-1 Guinier plot ln 3.64×103 Rg: 3.9 nm 0 (3.9 nm)-2 s2
Netrin-1 Kratky plot 1.104 0 3 sRg
Netrin-1 pair distance distribution function Rg: 4 nm 0 Dmax: 13.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Netrin-1 DAMMIN model

Synchrotron SAXS data from solutions of NetrinVIV in 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 1.2 mg/ml were measured at 10°C. 20 successive 0.050 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Netrin-1 (NetrinVIV)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   49.1 kDa
UniProt   O95631
Sequence   FASTA