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Related Experiment Videos

Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion.

P H Jensen1, V Soroka, N K Thomsen

  • 1Department of Chemistry, Carlsberg Laboratory, Valby, Denmark.

Nature Structural Biology
|May 20, 1999
PubMed
Summary

The structure of the second Neural Cell Adhesion Molecule (NCAM) Ig-module was determined. This fragment forms a stable dimer, crucial for neural cell adhesion interactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Neural Cell Adhesion Molecule (NCAM) is vital for cell interactions in the nervous system.
  • NCAM comprises multiple immunoglobulin (Ig)-like modules, each playing a role in its function.
  • Understanding the structural basis of NCAM interactions is key to deciphering neural development and function.

Purpose of the Study:

  • To determine the solution structure of the second Ig-module fragment (residues 117-208) of NCAM.
  • To investigate the interaction between the first and second Ig-modules of NCAM.
  • To elucidate the structural basis of NCAM dimerization and its implications for cell adhesion.

Main Methods:

  • X-ray crystallography or NMR spectroscopy to determine the structure of the NCAM Ig-module fragment.

Related Experiment Videos

  • Biochemical assays to study the interaction between module 1 and module 2.
  • Site-directed mutagenesis to identify key residues involved in dimerization.

    • Main Results:

    • The second Ig-module fragment (117-208) belongs to the I set of the immunoglobulin superfamily.
    • Weak interactions between module 1 and module 2 were identified, with specific binding sites pinpointed.
    • The two-module fragment NCAM(20-208) forms a stable dimer, and removal of charged residues abolishes this dimerization.
    • Modeling suggests a binding site facilitating antiparallel strands of the first two NCAM modules.

    Conclusions:

    • The determined structure provides insights into the molecular organization of NCAM.
    • The identified interaction sites and dimerization mechanism are critical for NCAM function.
    • This mode of binding likely plays a significant role in trans-cellular interactions during neural cell adhesion.