Structural basis of hepatocyte growth factor/scatter factor and MET signalling

Gherardi E, Sandin S, Petoukhov M, Finch J, Youles M, Ofverstedt L, Miguel R, Blundell T, Vande Woude G, Skoglund U, Svergun D, Proceedings of the National Academy of Sciences 103(11):4046-4051 (2006) DOI

SASDLQ7 – receptor tyrosine kinase MET

Hepatocyte growth factor receptor
MWexperimental 91 kDa
MWexpected 100 kDa
VPorod 190 nm3
log I(s) 1.52×102 1.52×101 1.52×100 1.52×10-1
Hepatocyte growth factor receptor small angle scattering data  s, nm-1
ln I(s)
Hepatocyte growth factor receptor Guinier plot ln 1.53×102 Rg: 4.8 nm 0 (4.8 nm)-2 s2
(sRg)2I(s)/I(0)
Hepatocyte growth factor receptor Kratky plot 1.104 0 √3 sRg
p(r)
Hepatocyte growth factor receptor pair distance distribution function Rg: 4.9 nm 0 Dmax: 16 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Hepatocyte growth factor receptor SASREF model
Synchrotron SAXS data from solutions of the receptor tyrosine kinase MET in 50 mM MES, 150 mM NaCl, pH 6.7 were collected on the EMBL X33 beam line at the DORIS III storage ring (DESY, Hamburg, Germany) using a 1D Gas detector detector at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.2 and 9.1 mg/ml were measured . 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.

Experimental temperature: UNKNOWN. X-ray exposure time: UNKNOWN.

Tags: X33
Hepatocyte growth factor receptor
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   100.3 kDa
 
UniProt   P16056 (25-927)
Sequence   FASTA