1ern
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Erythropoietin receptor (EPOR) is thought to be activated by | + | 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== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Livnah, O.]] | [[Category: Livnah, O.]] | ||
| - | [[Category: Stura, E | + | [[Category: Stura, E A.]] |
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: cytokine receptor class 1]] | [[Category: cytokine receptor class 1]] | ||
[[Category: erythropoietin receptor]] | [[Category: erythropoietin receptor]] | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:00 2008'' |
Revision as of 10:31, 21 February 2008
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NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]
Contents |
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
Page seeded by OCA on Thu Feb 21 12:31:00 2008
