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Article
Nature 360, 232 - 239 (19 November 1992); doi:10.1038/360232a0

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

E. Yvonne Jones*, Simon J. Davis, Alan F. Williams, Karl Harlos* & David I. Stuart*

*Laboratory of Molecular Biophysics, The Rex Richards Building, South Parks Road, Oxford OX1 3QU, UK
MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK

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 β-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.

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