Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2

Nature. 1992 Nov 19;360(6401):232-9. doi: 10.1038/360232a0.

Abstract

The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Differentiation, T-Lymphocyte / chemistry*
  • CD2 Antigens
  • Cell Adhesion Molecules / chemistry*
  • Crystallization
  • Epitopes / chemistry
  • Glycosylation
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Protein Structure, Tertiary
  • Rats
  • Receptors, Immunologic / chemistry*
  • X-Ray Diffraction

Substances

  • Antigens, Differentiation, T-Lymphocyte
  • CD2 Antigens
  • Cell Adhesion Molecules
  • Epitopes
  • Peptide Fragments
  • Receptors, Immunologic