1ERN
NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]
Summary for 1ERN
| Entry DOI | 10.2210/pdb1ern/pdb |
| Descriptor | PROTEIN (ERYTHROPOIETIN RECEPTOR) (2 entities in total) |
| Functional Keywords | erythropoietin receptor, signal transduction, cytokine receptor class 1, cytokine |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein. Isoform EPOR-S: Secreted: P19235 |
| Total number of polymer chains | 2 |
| Total formula weight | 47023.32 |
| Authors | Livnah, O.,Stura, E.A.,Wilson, I.A. (deposition date: 1999-01-11, release date: 2000-01-07, Last modification date: 2024-11-06) |
| Primary citation | Livnah, O.,Stura, E.A.,Middleton, S.A.,Johnson, D.L.,Jolliffe, L.K.,Wilson, I.A. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science, 283:987-990, 1999 Cited by PubMed Abstract: Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced homodimerization. However, structures of agonist and antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have shown that the actual dimer configuration is critical for the biological response and signal efficiency. The crystal structure of the extracellular domain of EPOR in its unliganded form at 2.4 angstrom resolution has revealed a dimer in which the individual membrane-spanning and intracellular domains would be too far apart to permit phosphorylation by JAK2. This unliganded EPOR dimer is formed from self-association of the same key binding site residues that interact with EPO-mimetic peptide and EPO ligands. This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors. PubMed: 9974392DOI: 10.1126/science.283.5404.987 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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