The erythropoietin receptor (EpoR) is a protein that in humans is encoded by the EPOR gene.[5] EpoR is a 52kDa peptide with a single carbohydrate chain resulting in an approximately 56-57 kDa protein found on the surface of EPO responding cells. It is a member of the cytokine receptor family. EpoR pre-exists as dimers. These dimers were originally thought to be formed by extracellular domain interactions,[6] however, it is now assumed that it is formed by interactions of the transmembrane domain[7][8] and that the original structure of the extracellular interaction site was due to crystallisation conditions and does not depict the native conformation.[9] Binding of a 30 kDa ligand erythropoietin (Epo), changes the receptor's conformational change, resulting in the autophosphorylation of Jak2 kinases that are pre-associated with the receptor (i.e., EpoR does not possess intrinsic kinase activity and depends on Jak2 activity).[10][11] At present, the best-established function of EpoR is to promote proliferation and rescue of erythroid (red blood cell) progenitors from apoptosis.[5]
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