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. 2015 Mar 24;10(3):e0122452. doi: 10.1371/journal.pone.0122452

Fig 1. Schematic representation of the hTfR-EGFP chimera.

Fig 1

TfR is a type II transmembrane glycoprotein found primarily as a homodimer consisting of identical monomers joined by two disulfide bonds. Each monomer (760 amino acids) consists of three major domains as follows: a large glycosylated extracellular C-terminal domain (amino acids 90–760) involved in ligand binding, a single-pass transmembrane domain (amino acids 62–89), and a short intracellular N-terminal domain (amino acids 1–61). The EGFP moiety is fused to the amino terminus of hTfR.