Fig. 1.
Fig. 1. Domain structure shows features unique to endogenous TPO. / The amino terminus (first 153 amino acids) of TPO contains 4 conserved cysteine residues and is 17% identical to erythropoietin (EPO; ∼50% identical if neutral substitutions are taken into account). It contains the entire receptor-binding region. The shaded boxes show the predicted α-helical regions of TPO. The carboxyl terminus (amino acids 154 to 332) of the molecule appears to be unique to TPO and contains theN-linked glycosylation sites indicated by solid arrows. Adapted from Foster and Hunt47 with permission.

Domain structure shows features unique to endogenous TPO.

The amino terminus (first 153 amino acids) of TPO contains 4 conserved cysteine residues and is 17% identical to erythropoietin (EPO; ∼50% identical if neutral substitutions are taken into account). It contains the entire receptor-binding region. The shaded boxes show the predicted α-helical regions of TPO. The carboxyl terminus (amino acids 154 to 332) of the molecule appears to be unique to TPO and contains theN-linked glycosylation sites indicated by solid arrows. Adapted from Foster and Hunt47 with permission.

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