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Fig. 1 | Molecular Neurodegeneration

Fig. 1

From: ApoE in Alzheimer’s disease: pathophysiology and therapeutic strategies

Fig. 1

Structural model of apoE highlighting AD-related amino acid variations. ApoE is a 299 amino acid glycoprotein with a molecular weight of 34 kDa (PDB 2L7B). It is formed of two independently folded domains linked by a hinge region: the N-terminal domain (residues 1-167) contains the receptor-binding region while the C-terminal domain (residues 206–299) includes the lipid-binding region. There are three major apoE isoforms that differ at amino acid positions 112 and 158: apoE2 (C112/C158); apoE3 (C112/R158); and apoE4 (R112/R158). Additional rare apoE variants have been identified: apoE3-Christchurch (R136S), apoE3-Jacksonville (apoE3-V236E), and apoE4-R251G

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