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Figure 1. Panel A: Model depicting the structures the two EPOR embedded into the membrane of
committed CFU-E progenitor cells. EPO, which is produced in the kidney and released into the blood-
stream, functions by binding two receptors, causing dimerization. The complex of EPO and two
EPOR allows the precise geometry required by intracellular portion of EPOR (not shown in this dia-
gram) for biologic activity. The relative proximity of the two intracellular regions caused by the
mechanical association of EPO with EPOR allows the association and phosphorylation of kinases,
which is the intiating event that allows the cell to mature into a red blood cell. Panel B: The X-ray
crystallographic structure of EPO bound to two EPOR. The structure resolved by Syed et al. [1] pro-
vides the empirical data about the details of the interaction between EPO and its natural receptors.
Figures courtesy of Timothy Osslund.
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