1ern

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[[Image:1ern.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1ern| PDB=1ern | SCENE= }}
{{STRUCTURE_1ern| PDB=1ern | SCENE= }}
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'''NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]'''
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===NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9974392}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9974392 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9974392}}
==About this Structure==
==About this Structure==
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[[Category: Erythropoietin receptor]]
[[Category: Erythropoietin receptor]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:26:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:46:07 2008''

Revision as of 22:46, 30 June 2008

Image:1ern.png

Template:STRUCTURE 1ern

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

Template:ABSTRACT PUBMED 9974392

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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