Sandbox Reserved 595: Difference between revisions

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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).

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).

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).

Sandbox Reserved 595: Difference between revisions

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Revision as of 01:01, 27 March 2013 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 01:13, 27 March 2013 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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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).

	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).		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).