1ERN

NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]

1ERN の概要

• エントリーDOI: 10.2210/pdb1ern/pdb
• 分子名称: PROTEIN (ERYTHROPOIETIN RECEPTOR) (2 entities in total)
• 機能のキーワード: erythropoietin receptor, signal transduction, cytokine receptor class 1, cytokine
• 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: 2
• 化学式量合計: 47023.32

構造登録者

Livnah, O.,Stura, E.A.,Wilson, I.A. (登録日: 1999-01-11, 公開日: 2000-01-07, 最終更新日: 2024-11-06)

主引用文献

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

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: 9974392
DOI: 10.1126/science.283.5404.987

実験手法

X-RAY DIFFRACTION (2.4 Å)