Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements.
As part of a continuing investigation of netrins, an emerging class of extracellular matrix proteins that are involved in axon guidance activity, we have used dynamic light scattering (DLS) and small angle X-ray scattering to investigate the solution conformation of a truncated version of netrin-4 (Δnetrin-4) that lacks the C-terminal portion. The protein is characterized by a hydrodynamic (Stokes) radius (r(H)) of 4.60 (±0.20) nm, a radius of gyration (r(G)) of 4.42 (±0.20) nm and a maximum particle dimension (D(max)) of 16nm. More detailed ab initio modeling of the SAXS data indicates an extended rod like conformation for Δnetrin-4 in solution-a concept supported by the excellent agreement observed between experimental parameter estimates and those calculated for the ab initio models for Δnetrin-4 by the HYDROPRO program.
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2.
Trushar R
TR
Patel
Raphael
R
Reuten
Shawn
S
Xiong
Markus
M
Meier
Donald J
DJ
Winzor
Manuel
M
Koch
Jörg
J
Stetefeld
D000818:Animals; D003198:Computer Simulation; D057446:Hydrodynamics; D046911:Macromolecular Substances / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D009414:Nerve Growth Factors / Q000737:chemistry*; D000075385:Netrins; D011487:Protein Conformation; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods*
D046911:Macromolecular Substances; D009414:Nerve Growth Factors; D000075385:Netrins; C416214:Ntn4 protein, mouse