Sandbox Reserved 595: Difference between revisions

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=Background=

Apolipoprotein E is a member of the apolipoprotein family. This soluble ~~apolipoprotein~~ is produced primarily in the liver and brain; and it is located principally in the plasma and in the central nervous system (CNS) (AA). The systemic transport of cholesterol and other lipids is this protein's ~~principle~~ role in the body (W). One minor function it may exhibit is that of immune regulation (W). Particular isoforms, ε2 and ε4 implicated in hyperlipoproteinemia (HLP III) and late onset Alzheimer's disease (LOAD). ~~ApoE may also play a role in synaptic integrity and plasticity (R).~~

Apolipoprotein E is a member of the apolipoprotein family. This soluble protein is produced primarily in the liver and brain; and it is located principally in the plasma and in the central nervous system (CNS) (AA). The systemic transport of cholesterol and other lipids is this protein's main role in the body (W). One minor function it may exhibit is that of immune regulation (W). ApoE may also play a role in synaptic integrity and plasticity (R). Particular isoforms, ε2 and ε4 are implicated in hyperlipoproteinemia (HLP III) and late onset Alzheimer's disease (LOAD).

=Structure=

==Primary Structural Features==

Apolipoprotein E is a polymorphic glycoprotein that consists of 299 amino acids (A,F). It has a molecular weight of 34kDa (G). The primary structure for ApoE is rich in the amino acid argine (W).

==Secondary Structural Features==

==Secondary & Tertiary Structural Features==

ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M). The amino terminal domain has a molecular weight of ~~2-kDa~~ and comprises the residues 1-199 (C,F,J,M). It is a globular domain consisting of an antiparallel bundle of 4 amphipathic alpha-helices, rich in basic amino acids; pronounced kinks are present in the helices near the end of the 4-helix bundle that corresponds with the protein's lipid binding ability (C,F,J,L). In the fourth helix, the residues between 145-150, known as the low density lipoprotein receptor binding region, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L).

ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M). The amino terminal domain has a molecular weight of 2kDa and comprises the residues 1-199 (C,F,J,M). It is a globular domain consisting of an antiparallel bundle of 4 amphipathic alpha-helices, rich in basic amino acids; pronounced kinks are present in the helices near the end of the 4-helix bundle that corresponds with the protein's lipid binding ability (C,F,J,L). In the fourth helix, the residues between 145-150, known as the low density lipoprotein receptor binding region, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L).

The carboxyl-terminal domain is 10kD respectively, and consists of the residues 216-299 (C,F). The C-terminal domain includes two kinds of amphipathic alpha helices. The first of these alpha helices is a class A helix.

Sandbox Reserved 595: Difference between revisions

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 =Background=
-Apolipoprotein E is a member of the apolipoprotein family.  This soluble apolipoprotein is produced primarily in the liver and brain; and it is located principally in the plasma and in the central nervous system (CNS) (AA).  The systemic transport of cholesterol and other lipids is this protein's principle role in the body (W).  One minor function it may exhibit is that of immune regulation (W).  Particular isoforms, ε2 and ε4 implicated in hyperlipoproteinemia (HLP III) and late onset Alzheimer's disease (LOAD).  ApoE may also play a role in synaptic integrity and plasticity (R).
+Apolipoprotein E is a member of the apolipoprotein family.  This soluble protein is produced primarily in the liver and brain; and it is located principally in the plasma and in the central nervous system (CNS) (AA).  The systemic transport of cholesterol and other lipids is this protein's main role in the body (W).  One minor function it may exhibit is that of immune regulation (W).  ApoE may also play a role in synaptic integrity and plasticity (R). Particular isoforms, ε2 and ε4 are implicated in hyperlipoproteinemia (HLP III) and late onset Alzheimer's disease (LOAD).
 =Structure=
 ==Primary Structural Features==
 Apolipoprotein E is a polymorphic glycoprotein that consists of 299 amino acids (A,F).  It has a molecular weight of 34kDa (G).  The primary structure for ApoE is rich in the amino acid argine (W).
-==Secondary Structural Features==
+==Secondary & Tertiary Structural Features==
-ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M).  The amino terminal domain has a molecular weight of 2-kDa and comprises the residues 1-199 (C,F,J,M).  It is a globular domain consisting of an antiparallel bundle of 4 amphipathic alpha-helices, rich in basic amino acids;  pronounced kinks are present in the helices near the end of the 4-helix bundle that corresponds with the protein's lipid binding ability (C,F,J,L).  In the fourth helix, the residues between 145-150, known as the low density lipoprotein receptor binding region, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L).
+ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M).  The amino terminal domain has a molecular weight of 2kDa and comprises the residues 1-199 (C,F,J,M).  It is a globular domain consisting of an antiparallel bundle of 4 amphipathic alpha-helices, rich in basic amino acids;  pronounced kinks are present in the helices near the end of the 4-helix bundle that corresponds with the protein's lipid binding ability (C,F,J,L).  In the fourth helix, the residues between 145-150, known as the low density lipoprotein receptor binding region, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L).
 The carboxyl-terminal domain is 10kD respectively, and consists of the residues 216-299 (C,F).  The C-terminal domain includes two kinds of amphipathic alpha helices.  The first of these alpha helices is a class A helix.