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Related Experiment Videos

Structure of the semaphorin-3A receptor binding module.

Alexander Antipenko1, Juha-Pekka Himanen, Klaus van Leyen

  • 1Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.

Neuron
|August 20, 2003
PubMed
Summary

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Researchers determined the crystal structure of Semaphorin-3A (Sema3A), revealing a novel beta propeller fold. This finding elucidates Sema3A

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Developmental Biology

Background:

  • Semaphorins are extracellular proteins crucial for neuronal development, including migration and axon guidance.
  • A conserved semaphorin domain mediates ligand-receptor interactions with plexins and scatter-factor receptors.

Purpose of the Study:

  • To determine the crystal structure of a secreted form of Semaphorin-3A (Sema3A).
  • To elucidate the structural basis of semaphorin signaling and identify key interaction sites.

Main Methods:

  • X-ray crystallography was used to determine the 65 kDa secreted form of Sema3A structure.
  • Structure-based mutagenesis was employed to identify binding sites.

Main Results:

Related Experiment Videos

  • The semaphorin domain exhibits an unexpected beta propeller fold.
  • The neuropilin binding site was identified, and a potential plexin interaction site was suggested.
  • A model for semaphorin signaling initiation was proposed.

    • Conclusions:

    • The crystal structure of Sema3A reveals a novel beta propeller fold.
    • Structural insights provide a basis for understanding semaphorin-neuropilin and semaphorin-plexin interactions.
    • The findings suggest potential similarities with signaling mechanisms of other beta propeller receptors.