1ern

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Revision as of 14:39, 12 November 2007

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spinqualitylabelsall models 1ern, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Erythrocytosis, familial OMIM:[133171]

About this Structure

1ERN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation., Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA, Science. 1999 Feb 12;283(5404):987-90. PMID:9974392

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