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Updated: Jan 20, 2026

A BW Reporter System for Studying Receptor-Ligand Interactions
Published on: January 7, 2019
Structural analysis of the transferrin receptor multifaceted ligand(s) interface
Claudia Testi1, Alberto Boffi2, Linda Celeste Montemiglio3
1Center for Life Nano Science @ Sapienza, Istituto Italiano di Tecnologia, V.le Regina Elena 291, Rome 00161, Italy.
Abstract:
The transferrin receptor 1 (TfR1) is one of the key regulators of iron homeostasis for most higher organisms. It mediates cellular iron import through a constitutive clathrin-dependent endocytosis mechanism and by recruiting iron- regulator proteins as transferrin, Hereditary Hemochromatosis factor (HFE) and serum ferritin in response to cellular demand. The receptor is also opportunistically exploited by several viruses and the malaria parasite as a preferential door for cell invasion. In this review, we analyze the structural information available for TfR1 and all its functional complexes to figure out how structural signals in a single receptor can guide the recognition of multiple ligands and how the conservation of key residues in TfR1 might have a role in iron uptake and cell infection.
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