1ern: Difference between revisions
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'''NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]'''<br /> | '''NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1ERN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1ERN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
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Revision as of 16:44, 15 February 2008
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NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Erythrocytosis, familial OMIM:[133171]
About this StructureAbout this Structure
1ERN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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