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1eba

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{{STRUCTURE_1eba| PDB=1eba | SCENE= }}
{{STRUCTURE_1eba| PDB=1eba | SCENE= }}
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'''COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)'''
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===COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)===
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==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.
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(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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:54:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:26:44 2008''

Revision as of 21:26, 30 June 2008

Image:1eba.png

Template:STRUCTURE 1eba

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

Template:ABSTRACT PUBMED 9808045

About this Structure

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

Reference

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation., Livnah O, Johnson DL, Stura EA, Farrell FX, Barbone FP, You Y, Liu KD, Goldsmith MA, He W, Krause CD, Pestka S, Jolliffe LK, Wilson IA, Nat Struct Biol. 1998 Nov;5(11):993-1004. PMID:9808045

Page seeded by OCA on Tue Jul 1 00:26:44 2008

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