1eba: Difference between revisions

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[[Image:1eba.gif|left|200px]]
{{Seed}}
[[Image:1eba.png|left|200px]]


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{{STRUCTURE_1eba|  PDB=1eba  |  SCENE=  }}  
{{STRUCTURE_1eba|  PDB=1eba  |  SCENE=  }}  


'''COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)'''
===COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)===




==Overview==
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Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands is the principal extracellular event that leads to receptor activation. The crystal structure of the extracellular domain of EPOR bound to an inactive (antagonist) peptide at 2.7 A resolution has unexpectedly revealed that dimerization still occurs, but the orientation between receptor molecules is altered relative to active (agonist) peptide complexes. Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.
The line below this paragraph, {{ABSTRACT_PUBMED_9808045}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9808045 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9808045}}


==About this Structure==
==About this Structure==
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[[Category: Protein minimization]]
[[Category: Protein minimization]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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