The conundrum of the high-affinity NGF binding site formation unveiled?

Covaceuszach S, Konarev PV, Cassetta A, Paoletti F, Svergun DI, Lamba D, Cattaneo A, Biophys J 108(3):687-97 (2015) Europe PMC

SASDLG5 – Human nerve growth factor

Beta-nerve growth factor
MWI(0) 33 kDa
MWexpected 24 kDa
log I(s) 1.54×102 1.54×101 1.54×100 1.54×10-1
Beta-nerve growth factor small angle scattering data  s, nm-1
ln I(s)
Beta-nerve growth factor Guinier plot ln 1.54×102 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Beta-nerve growth factor Kratky plot 1.104 0 3 sRg

Data validation


Fits and models


log I(s)
 s, nm-1
Beta-nerve growth factor PDB (PROTEIN DATA BANK) model
Beta-nerve growth factor GROMACS model

Synchrotron SAXS data from solutions of human nerve growth factor in 50 mM Na-phosphate, 1 mM EDTA, pH 7 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.77 mg/ml was measured at 20°C. Two successive 120 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.

This entry displays an example SAXS profile at 3.77 mg/ml that is best described as a dimer-of-dimer equilibrium of hNGF, with the corresponding volume fractions of 62.3 and 37.7, respectively. Protein hNGF undergoes concentration dependent oligomerization. The full concentration series data (spanning 0.43-5.50 mg/ml) and the respective oligomeric analyses are made available in the full-entry zip archive.

Tags: X33
Beta-nerve growth factor (NGF)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   12.2 kDa
 
UniProt   P01138 (131-239)
Sequence   FASTA
 
PDB ID   1BTG
 
PDB ID   1BTG