Analysis of the structure and interactions of CD2
Davis SJ, Jones EY, Bodian DL, Barclay AN, van der Merwe PA. (1993), Biochem Soc Trans. 21, 952-8
Key figure: Structural features and dimensions of the cell adhesion molecule CD2
The crystal structure of the extracellular region of rat CD2  is shown linked to the transmembrane sequence  modelled as an α-helix. The cytoplasmic domain of CD2 is 116 amino acids long and is relatively rich in proline and charged residues. However, no structural information exists for this region of the molecule and therefore this domain is omitted. The structure is shown in space filling format, using the program MOPE (D.I. Stuart, unpublished work), with the line of view parallel to the plane of the GFCC’C” β-sheet of domain 1. Three asparagine residues that are likely to be glycosylated and can be seen in this view are shown in black. To illustrate the probable relationship of CD2 with the cell surface, the lipid bilayer is shown diagrammatically with polar regions represented as circles or ovals and hydrocarbon chains as single lines; the dimensions of the bilayer are as described by Hauser et al. .