CRYSTAL-STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF RECEPTOR-HUMAN TNF-BETA COMPLEX - IMPLICATIONS FOR TNF RECEPTOR ACTIVATION
CRYSTAL-STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF RECEPTOR-HUMAN TNF-BETA COMPLEX - IMPLICATIONS FOR TNF RECEPTOR ACTIVATION
复制标题
DOI：
10.1016/0092-8674(93)90132-a
复制
发表时间：
1993-05-07
期刊：
影响因子：
64.5
通讯作者：
LESSLAUER, W
中科院分区：
文献类型：
--
作者：
BANNER, DW;DARCY, A;LESSLAUER, W
在2.85埃分辨率下测定了人55kd肿瘤坏死因子受体胞外区与人肿瘤坏死因子β的复合体的X射线晶体结构。该复合体有三个受体分子对称地结合在一个肿瘤坏死因子β三聚体上。受体片段是由四个相似的折叠结构域组成的非常细长的端到端组装，结合在两个相邻的TNFβ亚基之间的沟槽中。该复合体的结构确定了配体相对于细胞膜的方向，并为肿瘤坏死因子受体的激活提供了一个模型。肿瘤坏死因子受体结构的新折叠很可能是神经生长因子/肿瘤坏死因子受体家族的代表。
The X-ray crystal structure of the complex of the extracellular domain of the human 55 kd tumor necrosis factor (TNF) receptor with human TNFbeta has been determined at 2.85 angstrom resolution. The complex has three receptor molecules bound symmetrically to one TNFbeta trimer. The receptor fragment, a very elongated end to end assembly of four similar folding domains, binds in the groove between two adjacent TNFbeta subunits. The structure of the complex defines the orientation of the ligand with respect to the cell membrane and provides a model for TNF receptor activation. The novel fold of the TNF receptor structure is likely to be representative of the nerve growth factor (NGF)/TNF receptor family as a whole.