Structure of human hephaestin reveals a homodimer anchored to the cell membrane

Full-length human hephaestin was purified and imaged by cryo-EM, revealing a stable homodimer with well-resolved extracellular domains at ~2.3 Å overall resolution.

• Why it matters: Hephaestin is a membrane-bound ferroxidase required for exporting Fe2+ from ferroportin, yet full-length structural information has been missing, limiting understanding of its mechanism and Fpn interaction.
• What they did: The team expressed and purified functional full-length human Heph and determined its structure using cryo-electron microscopy, achieving an overall resolution of approximately 2.3 Å.
• The result: The structure shows a stable homodimer, defines transmembrane helix positions, and links a substrate-binding site to an electronegative funnel that may help Fe2+ capture, constraining models of Fpn interaction.

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