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Sandbox Reserved 595

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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 is comprised of the amino acid 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 is comprised of the amino acid 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).
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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 (residues 216-266) and the second is a class G helix (residues 273-299) (D).
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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 (residues 216-266) and the second is a class G helix (residues 273-299) (D). Residues 230-270 in the C-terminal domain are crucial for oliomer formation, self-aggregation (M). Those residues that are important for the initiation of lipid binding to ApoE are 261-272 (M).

Revision as of 01:13, 27 March 2013

This Sandbox is Reserved from Feb 1, 2013, through May 10, 2013 for use in the course "Biochemistry" taught by Irma Santoro at the Reinhardt University. This reservation includes Sandbox Reserved 591 through Sandbox Reserved 599.
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I would like the page to have a table of contents and the following main sections: Background, Structure (with a jmol image area), Function, Clinical Relevance, and References.

Contents

Background

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 & 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 2kDa and is comprised of the amino acid 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 (residues 216-266) and the second is a class G helix (residues 273-299) (D). Residues 230-270 in the C-terminal domain are crucial for oliomer formation, self-aggregation (M). Those residues that are important for the initiation of lipid binding to ApoE are 261-272 (M).

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