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)

1EBA の概要

• エントリーDOI: 10.2210/pdb1eba/pdb
• 分子名称: PROTEIN (ERYTHROPOIETIN RECEPTOR), PROTEIN (EPO MIMETICS PEPTIDE 33) (2 entities in total)
• 機能のキーワード: erythropoietin receptor, signal transduction, protein minimization, drug design, cytokine receptor class 1, complex (cytokine receptor-peptide), signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein. Isoform EPOR-S: Secreted: P19235
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51990.15

構造登録者

Livnah, O.,Stura, E.A.,Wilson, I.A. (登録日: 1998-10-02, 公開日: 1998-11-11, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)