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Intrinsic structural disorder of mouse proNGF.

Francesca Paoletti1, Sonia Covaceuszach, Peter V Konarev

  • 1SISSA-ISAS, Building Q1, Area Science Park - Basovizza, S.S 14 Km 163.5, 34012 Trieste, Italy. f.paoletti@ebri.i

Proteins
|December 18, 2008
PubMed
Summary

The precursor Nerve Growth Factor (proNGF) has distinct functions from mature NGF due to its unstructured propeptide domain. This domain exhibits promiscuous binding to receptors and antibodies, influencing proNGF

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • The unprocessed precursor of Nerve Growth Factor (NGF), known as proNGF, possesses functions beyond its role in NGF folding.
  • ProNGF exhibits distinct apoptotic and/or neurotrophic properties compared to mature NGF, but the structural basis for these differences is unknown.

Purpose of the Study:

  • To elucidate the structural and molecular basis for the distinct biological activities of proNGF compared to mature NGF.
  • To investigate the specific molecular interactions governing proNGF's unique functions.

Main Methods:

  • Synchrotron small-angle X-ray scattering (SAXS) was employed to study proNGF structure in solution.
  • Surface plasmon resonance (SPR) was used to analyze binding properties with anti-NGF antibodies and TrkA/p75(NTR) receptors.

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Main Results:

  • SAXS revealed proNGF as a dimeric, isometric molecule with an intrinsically unstructured propeptide domain.
  • Structural modeling suggested a "crab-like" conformation as more likely for proNGF.
  • SPR data indicated that the proNGF propeptide exhibits promiscuous binding to multiple partners, including TrkA and p75(NTR) receptors.

Conclusions:

  • The intrinsically unstructured propeptide domain of proNGF is key to its distinct biological activities and promiscuous binding.
  • These findings offer initial insights into the structural basis for proNGF's selective interactions with its binding partners.