Sandbox Reserved 595: Difference between revisions

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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 correspond 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). This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/1'>residues 112 and 158</scene>, which are responsible for much of the differences between the three isoforms of apoE. 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 correspond 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). It presents a large exposed hydrophobic surface that is well-suited for interacting with multiple binding partners, including lipids, heparin sulfate proteoglycans (HSPGs), and amyloid beta peptides (Aβ) (V). This domain harbors high-affinity lipid binding properties and is therefore capable of anchoring lipoprotein particles; it also contains sites that mediate ApoE self-association (C,D,I,J,P). 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 oligomer formation(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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@@ Line 13: / Line 13: @@
 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 correspond 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).  This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/1'>residues 112 and 158</scene>, which are responsible for much of the differences between the three isoforms of apoE.  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 correspond 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).  It presents a large exposed hydrophobic surface that is well-suited for interacting with multiple binding partners, including lipids, heparin sulfate proteoglycans (HSPGs), and amyloid beta peptides (Aβ) (V).  This domain harbors high-affinity lipid binding properties and is therefore capable of anchoring lipoprotein particles; it also contains sites that mediate ApoE self-association (C,D,I,J,P).  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 oligomer formation(M).  Those residues that are important for the initiation of lipid binding to ApoE are 261-272 (M).