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Structural basis for the signal transduction of erythropoietin

  • Timothy D. Osslund
Part of the Milestones in Drug Therapy book series (MDT)

Abstract

The structures of recombinant erythropoietin (r-HuEPO), the extracellular ligand-binding portion of erythropoietin receptor (EPOR) and several novel peptides have been extensively studied using a variety of methods including X-ray crystallography and nuclear magnetic resonance (NMR) [1, 2] The receptor for EPO has been classified as a member of the class 1 cytokine receptor super family [3, 4]. EPOR is a transmembrane receptor that is activated when EPO binds to the extracellular portion of the receptor causing dimerization [5]. The dimerization of the extracellular portion of the receptor induces tyrosine kinase proteins associated with the cytoplasmic side of the receptor to initiate the signal transduction events that eventually cause the committed erythroid-colony-forming units (CFU-E) progenitor cells to eventually mature into red blood cells [6] (Fig. 1).

Keywords

Darbepoetin Alfa Nuclear Magnetic Resonance Structure Erythropoietin Receptor Signal Transduction Event Extracellular Portion 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Birkhäuser Verlag/Switzerland 2009

Authors and Affiliations

  • Timothy D. Osslund
    • 1
  1. 1.Analytical and Formulation ScienceAmgen Inc.Thousand OaksUSA

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