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Structural insights into SorCS2-Nerve Growth Factor complex formation.

Nadia Leloup1, Lucas M P Chataigner1, Bert J C Janssen2

  • 1Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Faculty of Science, Utrecht University, 3584 CH, Utrecht, The Netherlands.

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Summary
This summary is machine-generated.

This study reveals the SorCS2 receptor structure, showing how it binds to neurotrophin ligands. This provides insights into neuronal plasticity and potential mental disorder mechanisms.

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Molecular Biology

Background:

  • SorCS receptors mediate signaling by proneurotrophin ligands, influencing neuronal plasticity, apoptosis, and mental disorders.
  • The structural basis for SorCS2 ectodomain function and ligand specificity remains largely unknown.

Purpose of the Study:

  • To elucidate the molecular structure of the SorCS2 receptor and its complex with Nerve Growth Factor (NGF).
  • To understand the extracellular specificity and structural plasticity of SorCS2 in ligand binding.

Main Methods:

  • X-ray crystallography was used to determine the structures of unliganded SorCS2 ectodomain and the SorCS2-NGF complex.
  • Biophysical experiments were conducted to confirm ligand binding interactions.

Main Results:

  • Crystal structures revealed SorCS2 forms cross-braced homodimers with a 2:4 stoichiometry of NGF dimers.
  • A C-terminal domain with an RNA recognition motif fold locks the dimer structure.
  • The SorCS2 β-propeller domain serves as the primary platform for binding NGF, proNGF, and proBDNF, with significant conformational flexibility observed.

Conclusions:

  • The SorCS2 receptor exhibits substantial structural plasticity, utilizing its β-propeller domain for ligand recognition.
  • These findings offer a structural framework for understanding SorCS2-mediated signaling in neuronal function and disease.