CRYSTAL-STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF A SOLUBLE FORM OF THE CELL-ADHESION MOLECULE CD2
CRYSTAL-STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF A SOLUBLE FORM OF THE CELL-ADHESION MOLECULE CD2
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DOI：
10.1038/360232a0
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发表时间：
1992-11-19
期刊：
影响因子：
64.8
通讯作者：
STUART, DI
中科院分区：
文献类型：
--
作者：
JONES, EY;DAVIS, SJ;STUART, DI
可溶性T淋巴细胞抗原CD2的晶体结构提供了细胞粘附分子胞外区的第一个完整视图。该分子的拓扑结构，其包含两个免疫球蛋白样结构域，与CD4的前两个结构域的拓扑结构相同，但相对结构域取向被相当灵活的接头区改变。假定的配体结合β-折叠形成朝向分子顶部的平坦表面。这些表面之间的晶体接触提出了一个合理的模型的粘合剂的相互作用。
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.