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Related Experiment Videos

The sema domain.

Ermanno Gherardi1, Christopher A Love, Robert M Esnouf

  • 1MRC Centre, Hills Road, Cambridge CB2 2QH, UK. egherard@mrc-lmb.cam.ac.uk

Current Opinion in Structural Biology
|December 8, 2004
PubMed
Summary
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The sema domain, crucial for semaphorins, plexin receptors, and MET/RON kinases, has a conserved beta-propeller fold. Structural analysis reveals plasticity in ligand-receptor interactions, explaining diverse functions in development and disease.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Developmental Biology

Background:

  • The sema domain is a key structural and functional component of semaphorins, plexin receptors, and receptor tyrosine kinases (MET, RON).
  • These protein families play critical roles in biological processes including development, tissue regeneration, and cancer.
  • Previous understanding of the sema domain was primarily based on sequence homology.

Purpose of the Study:

  • To analyze the structural basis of the sema domain's function.
  • To investigate the structural differences and similarities among semaphorin, plexin, MET, and RON families.
  • To understand how sema domain structure relates to ligand-receptor specificity and function.

Main Methods:

  • X-ray crystallography was used to determine the structures of two semaphorins (SEMA3A, SEMA4D) and the MET receptor.

Related Experiment Videos

  • Comparative structural analysis of the determined structures.
  • Sequence analysis to identify conserved regions within the sema domain.

    • Main Results:

    • The sema domain adopts a conserved seven-blade beta-propeller fold across different protein families.
    • Structural data revealed variations in dimerization modes among semaphorins, plexins, MET, and RON.
    • Specific regions involved in ligand-receptor interactions differ, indicating adaptive plasticity of the sema domain.

    Conclusions:

    • The sema domain's conserved fold provides a stable platform, while its plasticity allows for diverse binding requirements.
    • Structural variations explain the broad range of ligand-receptor specificities within the semaphorin superfamily.
    • Understanding sema domain structure-function relationships is vital for research in development, regeneration, and cancer therapy.