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. Author manuscript; available in PMC: 2010 Jul 22.
Published in final edited form as: Nat Rev Neurosci. 2009 Apr 2;10(5):333–344. doi: 10.1038/nrn2620

Figure 1. Schematic representation of human apoE.

Figure 1

The 299-amino acid human apoE contains two independently folded domains: an N-terminal domain that includes the receptor-binding region and a C-terminal domain that contains the major lipid-binding region. The residues that distinguish the apoE isoforms (112 and 158) are marked. ApoE2 has cysteines at both positions, apoE4 has arginines at both positions, and apoE3 has Cys at position 112 and Arg at position 158. Domain interaction between Arg61 and Glu255 in apoE4 is also indicated.