Apolipoprotein E: Structure-Function Relationships

In the citing paper

“We identified Gly145Asp and Arg154Cys in the same J o u r n a l P r e -p r o o f region (amino acids ~ 148 to 168) [47]”

In the citing paper

“Variants predicted by models to be deleterious or being located near or in the receptor binding region (amino acids ~ 148 to 168) [47] could be suspected to pose ε2-like qualities.”

In the citing paper

“Additional support comes from the present data, where Gly145Asp and Arg154Cys are located in the receptor binding region (amino acids ≈148 to 168) 28 and display a phenotype similar to the ɛ2‐defining Arg176Cys residue with high apoE levels and seemingly low risk of dementia (no events).”

In the citing paper

“Val254Glu and Arg269Gly are located in the lipid‐binding carboxyl‐terminal domain (amino acids ≈243 to 317). 28 , 42”

In the citing paper

“However, the receptor-binding sites (AA136-150) for lipoprotein receptors such as the low-density lipoprotein receptor (LDLR), lipoprotein-related receptor 1 (LRP1), and heparan sulfate proteoglycans (HSPGs) are located in a region conserved between species (Fig. 1a) [11–14].”

In the citing paper

“Notably, an HSPG and LDLR binding site in the APOE sequence is conserved in mice (blue boxed area, AA136-150), including arginine 136, which is replaced by serine in the Christchurch (Ch) variant [12, 39].”

In the citing paper

“However, mAPOE and hAPOE have a conserved LDLR and HSPG binding motif between AA136 to 150 (human numbering) [11, 12, 39], which includes the R136S Christchurch variant.”

In the citing paper

“The mature apoE protein consists of 299 amino acids and an 18amino acid signal peptide is removed post-translationally [17,28].”

In the citing paper

“The APOE gene is located on chromosome 19 and consists of four exons [28].”

In the citing paper

“Lipid-free apoE consists of two domains connected by a “hinge region”: the amino-terminal domain (amino acids 1 to 191) contains the receptor-binding function and the carboxyl-terminal domain (~amino acids 225 to 299) contains the lipid-binding function [28,33].”

In the citing paper

“The low density lipoprotein (LDL) receptor binding region is situated in helix four between amino acids 136 and 150 [17,28].”

In the citing paper

“ApoE2 exhibits a lower affinity to the LDL receptor compared to apoE3: ~1% of the binding activity of apoE3 and apoE4 [28,36].”

In the citing paper

“Furthermore, apoE and apoB share the sequence with highest affinity for arterial proteoglycans, a key phenomenon for lipoprotein deposition in the arterial wall [28,63].”

In the citing paper

“ApoE contains two independently folded functional domains; these are a 22-kDa N-terminal domain (residues 1–191) and a 10-kDa C-terminal domain (residues 216–299) linked by a hinge region (18, 19).”