Jones E Y, Davis S J, Williams A F, Harlos K, Stuart D I
Laboratory of Molecular Biophysics, Oxford, UK.
Nature. 1992 Nov 19;360(6401):232-9. doi: 10.1038/360232a0.
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.
T淋巴细胞抗原CD2可溶性形式的晶体结构首次完整展现了细胞粘附分子的细胞外区域。该分子由两个免疫球蛋白样结构域组成,其拓扑结构与CD4的前两个结构域相同,但相对结构域方向因一个相当灵活的连接区而改变。假定的配体结合β折叠在分子顶部形成一个平面。这些表面之间的晶体接触为粘附相互作用提出了一个合理的模型。