1TNR
CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF RECEPTOR-HUMAN TNF-BETA COMPLEX: IMPLICATIONS FOR TNF RECEPTOR ACTIVATION
Summary for 1TNR
| Entry DOI | 10.2210/pdb1tnr/pdb |
| Descriptor | TUMOR NECROSIS FACTOR BETA, TUMOR NECROSIS FACTOR RECEPTOR P55 (3 entities in total) |
| Functional Keywords | complex(lymphokine-receptor), complex(lymphokine-receptor) complex, complex(lymphokine/receptor) |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: P01374 Cell membrane; Single-pass type I membrane protein: P19438 |
| Total number of polymer chains | 2 |
| Total formula weight | 31639.70 |
| Authors | Banner, D.W. (deposition date: 1994-05-09, release date: 1994-07-31, Last modification date: 2024-10-16) |
| Primary citation | Banner, D.W.,D'Arcy, A.,Janes, W.,Gentz, R.,Schoenfeld, H.J.,Broger, C.,Loetscher, H.,Lesslauer, W. Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell(Cambridge,Mass.), 73:431-445, 1993 Cited by PubMed Abstract: The X-ray crystal structure of the complex of the extracellular domain of the human 55 kd tumor necrosis factor (TNF) receptor with human TNF beta has been determined at 2.85 A resolution. The complex has three receptor molecules bound symmetrically to one TNF beta trimer. The receptor fragment, a very elongated end to end assembly of four similar folding domains, binds in the groove between two adjacent TNF beta 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. PubMed: 8387891DOI: 10.1016/0092-8674(93)90132-a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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