Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.
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.
D000595:Amino Acid Sequence; D000818:Animals; D000945:Antigens, Differentiation, T-Lymphocyte / Q000737:chemistry*; D018801:CD2 Antigens; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D003460:Crystallization; D000939:Epitopes / Q000737:chemistry; D006031:Glycosylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D017434:Protein Structure, Tertiary; D051381:Rats; D011971:Receptors, Immunologic / Q000737:chemistry*; D014961:X-Ray Diffraction
D000945:Antigens, Differentiation, T-Lymphocyte; D018801:CD2 Antigens; D015815:Cell Adhesion Molecules; D000939:Epitopes; D010446:Peptide Fragments; D011971:Receptors, Immunologic