Apolipoproteins E3 and E4, proteins with a molecular mass of 34.15 kDa, differ by a single amino acid change. ApoE4 contains an arginine residue at position 112, whereas apoE3 has a cysteine at this position. ApoE4 is the major risk factor for ...

The APOE gene encodes a 34.15 kDa plasma glycoprotein (299-amino acids) having receptor-binding region at N-terminal domain (1-164 residues) and lipid-binding region at C-terminal domain...

The residues that distinguish the apoE isoforms are in the N-terminus (apoE4, arginine 112; apoE3 and apoE2, cysteine 112). However, the lipid-binding region is in the C-terminus (residues 244–272).

Cysteine at position 158 (C158) in APOE2 is thought to cause deficient receptor binding, while arginine at position 112 (R112) in APOE4 changes the conformation of the entire domain such that...

The APOE gene (located at 19q13.2) encodes a glycoprotein (34kDa) that is composed of 299 amino acids (apoE) and is associated with low-density lipoproteins (LDL), very-low-density...

The cysteine-to-arginine substitution in apoE2 at position 158 affects receptor-binding activity by eliminating a salt bridge between Arg158 and Asp154 and by forming of a new salt bridge between Arg150 and Asp154 .

2006年8月1日 · The cysteine-to-arginine substitution in apoE2 at position 158 affects receptor-binding activity by eliminating a salt bridge between Arg158 and Asp154 and by forming of a new salt bridge between Arg150 and Asp154 [26].

2017年8月1日 · The present review examines the current knowledge on APOE gene structure, phylogeny and APOE protein topology as well as its human isoforms. The ε4 allele is associated with an increased age-related disease risk but is also the ancestral form.

The presence of cysteine or arginine at position 158 affects a key salt-bridge arrangement in apoE3 and apoE2, resulting in a different position of Arg150 that alters its ability to interact effectively with LDL receptors.

Arg150 could relocate within the receptor-binding region. 2 APOE ε3 allele presents a cysteine in position 112 and arginine in position 158. 1. Arg112 mediates two key features of the ε4 allele, as it is associated with reduced stability. The ε4 allele could promote the domain interaction by the orientation of Arg61 on the N-terminal domain.