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Related Experiment Videos

Structural basis of cell-cell adhesion by NCAM.

C Kasper1, H Rasmussen, J S Kastrup

  • 1Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100 Copenhagen O, Denmark.

Nature Structural Biology
|May 10, 2000
PubMed
Summary

Neural cell adhesion molecule (NCAM) facilitates cell recognition and adhesion. Its crystal structure reveals a cross-shaped dimer, explaining how NCAM mediates cell-cell interactions in the nervous system.

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Molecular Biology

Background:

  • Neural cell adhesion molecule (NCAM) is crucial for nervous system development, regeneration, and synaptic plasticity.
  • NCAM belongs to the immunoglobulin superfamily and mediates cell-cell recognition through homophilic interactions.

Purpose of the Study:

  • To determine the crystal structure of the N-terminal extracellular domains of NCAM.
  • To provide a structural basis for NCAM's homophilic interaction and cell recognition mechanisms.

Main Methods:

  • X-ray crystallography at 1.85 A resolution.
  • Analysis of the molecular packing and quaternary structure of the NCAM domains.

Main Results:

  • The crystal structure of the two N-terminal extracellular domains of NCAM was determined.

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  • The structure revealed a cross-shaped antiparallel dimer formed by NCAM molecules.
  • This dimeric structure provides insights into the trans-cellular recognition mediated by NCAM.

    • Conclusions:

    • The reported crystal structure offers a fundamental understanding of NCAM-mediated homophilic interactions.
    • This structural insight is key to comprehending NCAM's role in neural development, regeneration, and synaptic function.