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1ern
From Proteopedia
| 1ern, resolution 2.40Å () | |||||||||
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| Domains: | EpoR_lig-bind, FN3 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP]
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ERN is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science. 1999 Feb 12;283(5404):987-90. PMID:9974392
Page seeded by OCA on Tue Feb 17 21:46:48 2009
