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Related Experiment Videos

The structural biology of CD2.

P Moingeon1, H C Chang, P H Sayre

  • 1Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA.

Immunological Reviews
|October 1, 1989
PubMed
Summary

The CD2 molecule on T lymphocytes mediates adhesion and activation by interacting with LFA-3. Its structure and gene organization are conserved between humans and mice, with adhesion modulated by surface copy number.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The CD2 molecule is a transmembrane glycoprotein found on T lymphocytes.
  • It plays crucial roles in cell adhesion and activation.
  • CD2 interacts with LFA-3 to facilitate T-cell interactions.

Purpose of the Study:

  • To elucidate the structure and function of the CD2 molecule.
  • To investigate the molecular mechanisms of CD2-mediated adhesion and activation.
  • To compare the structure and gene organization of human and mouse CD2.

Main Methods:

  • Microchemical analysis of immunoaffinity-purified human CD2.
  • cDNA and genomic cloning of mouse and human CD2.
  • Analysis of transduction events using patch-clamp recordings.

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Main Results:

  • Human CD2 consists of 327 amino acids with distinct extracellular, transmembrane, and cytoplasmic domains.
  • The CD2 gene spans approximately 12 Kb and is organized into five exons.
  • CD2-mediated adhesion is likely modulated by alterations in surface CD2 copy number, not intracellular mechanisms.

Conclusions:

  • CD2's structure and gene organization are conserved across species.
  • CD2-mediated T-cell activation synergizes with T-cell receptor (TCR) signals.
  • Adhesion via CD2 is primarily regulated by surface expression levels.