Figure 1
From: The transmembrane domains mediate oligomerization of the human ZIP4 transporter in vivo
The topology of ZIP4 (A) and truncated ZIP4 (B), the sequence alignment of ZIP transmembrane domain (TMD) 4 & 5 (C), and the computational study of ZIP4 transmembrane (D). (A) The full-length ZIP4 has eight transmembrane (TM1 to TM8) segments crossing the plasma membrane with a large N-terminus (1–327 residues) and C-terminus facing the extracellular environment. (B) The N-terminus (1–327 residues) has been removed from the full-length ZIP4 at the spot indicated by figure (A), the membrane domain (B) known as the truncated ZIP4. (C) Sequence alignment of human ZIP proteins TMD4 and TMD5. Conserved residues involved in metal coordination/translocation are highlighted in green. The computational study of ZIP4 transmembrane top and side views (D). The key residues for Zn2+ transport are colored in red.
