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The structure, organization, activation and plasticity of the erythropoietin receptor

Academic Article
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Overview

authors

  • Wilson, Ian
  • Jolliffe, L. K.

publication date

  • December 1999

journal

  • Current Opinion in Structural Biology  Journal

abstract

  • Dimerization of the erythropoietin receptor has long been accepted as the singular step in its mechanism of activation. Recent studies have revealed a regulator process for activation that is dependent on the actual configuration of the receptor-ligand dimer assembly. This aspect of the receptor subunit assembly appears to extend to the unliganded receptor, which can dimerize on the cell surface and diminish any spontaneous background signaling in the absence of ligand. This self-recognition, as well as the multiple ligand binding capabilities of the receptor binding site, is consistent with an emerging theme of plasticity in protein-protein and ligand-receptor interactions.

subject areas

  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Receptors, Erythropoietin
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Identity

International Standard Serial Number (ISSN)

  • 0959-440X

Digital Object Identifier (DOI)

  • 10.1016/s0959-440x(99)00032-9

PubMed ID

  • 10607675
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Additional Document Info

start page

  • 696

end page

  • 704

volume

  • 9

issue

  • 6

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