1EBA

COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)

Summary for 1EBA

• Entry DOI: 10.2210/pdb1eba/pdb
• Descriptor: PROTEIN (ERYTHROPOIETIN RECEPTOR), PROTEIN (EPO MIMETICS PEPTIDE 33) (2 entities in total)
• Functional Keywords: erythropoietin receptor, signal transduction, protein minimization, drug design, cytokine receptor class 1, complex (cytokine receptor-peptide), signaling protein
• 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: 4
• Total formula weight: 51990.15

Authors

Livnah, O.,Stura, E.A.,Wilson, I.A. (deposition date: 1998-10-02, release date: 1998-11-11, Last modification date: 2024-10-30)

Primary citation

Livnah, O.,Johnson, D.L.,Stura, E.A.,Farrell, F.X.,Barbone, F.P.,You, Y.,Liu, K.D.,Goldsmith, M.A.,He, W.,Krause, C.D.,Pestka, S.,Jolliffe, L.K.,Wilson, I.A.
An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation.
Nat.Struct.Biol., 5:993-1004, 1998

PubMed Abstract: Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands is the principal extracellular event that leads to receptor activation. The crystal structure of the extracellular domain of EPOR bound to an inactive (antagonist) peptide at 2.7 A resolution has unexpectedly revealed that dimerization still occurs, but the orientation between receptor molecules is altered relative to active (agonist) peptide complexes. Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.

PubMed: 9808045
DOI: 10.1038/2965

Experimental method

X-RAY DIFFRACTION (2.7 Å)