Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation

DW Banner, A D'Arcy, W Janes, R Gentz… - Cell, 1993 - cell.com
DW Banner, A D'Arcy, W Janes, R Gentz, HJ Schoenfeld, C Broger, H Loetscher…
Cell, 1993cell.com
The X-ray crystal structure of the complex of the extracellular domain of the human 55 kd
tumor necrosis factor (TNF) receptor with human TNFf3 has been determined at 2.85 A
resolution. The complex has three receptor molecules bound symmetrically to one TNF8
trimer. The receptor fragment, a very elongated end to end assembly of four similar folding
domains, binds in the groove between two adjacent TNFp subunits. The structure of the
complex defines the orientation of the ligand with respect to the ceil membrane and provides …
Summary
The X-ray crystal structure of the complex of the extracellular domain of the human 55 kd tumor necrosis factor (TNF) receptor with human TNFf3 has been determined at 2.85 A resolution. The complex has three receptor molecules bound symmetrically to one TNF8 trimer. The receptor fragment, a very elongated end to end assembly of four similar folding domains, binds in the groove between two adjacent TNFp subunits. The structure of the complex defines the orientation of the ligand with respect to the ceil 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.
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