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Related Experiment Videos

Structural and binding analysis of a two domain extracellular CD2 molecule.

P H Sayre1, R E Hussey, H C Chang

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

The Journal of Experimental Medicine
|March 1, 1989
PubMed
Summary

Researchers produced a soluble CD2 (T11) protein to study T cell adhesion. This recombinant protein, T11ex2, binds to LFA-3, revealing insights into the structure-function of T cell surface glycoproteins.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • The CD2 (T11) surface glycoprotein is crucial for human T lymphocyte and thymocyte activation and adhesion.
  • CD2 interacts with its ligand, LFA-3, mediating key cellular processes.

Purpose of the Study:

  • To investigate the structure-function relationships of the extracellular segment of the CD2 molecule.
  • To produce and characterize a recombinant soluble CD2 protein.

Main Methods:

  • Utilized a eukaryotic expression system and CD2 cDNA to generate recombinant soluble CD2.
  • Analyzed the protein's behavior in solution using biophysical techniques like circular dichroism.
  • Assessed the binding affinity of the recombinant protein to its ligand, LFA-3.

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Main Results:

  • Successfully produced milligram quantities of recombinant soluble CD2 (T11ex2) corresponding to the two extracellular exons.
  • T11ex2 exists as a monomer in solution and contains a stable N-terminal domain (domain I).
  • Circular dichroism indicated that domain II's secondary structure is stabilized by disulfide bonds.
  • The T11ex2 monomer exhibited a dissociation constant of 0.4 microM for LFA-3 binding.

Conclusions:

  • The recombinant T11ex2 protein provides a tool to study CD2 structure-function.
  • The relatively low affinity of monomeric T11ex2 to LFA-3 suggests cooperative binding is essential for physiological T cell adhesion.