1eba
From Proteopedia
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| - | [[Image:1eba.gif|left|200px]] | + | [[Image:1eba.gif|left|200px]] |
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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)''' | + | {{Structure |
| + | |PDB= 1eba |SIZE=350|CAPTION= <scene name='initialview01'>1eba</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''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== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EBA is a [ | + | 1EBA is a [[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=1EBA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9808045 9808045] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:02 2008'' |
Revision as of 08:53, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)
Contents |
Overview
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.
Disease
Known disease associated with this structure: Erythrocytosis, familial OMIM:[133171]
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
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