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 <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, 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 134-150, 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). This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE.

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 <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, 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 134-150, known as the <scene name='Sandbox_Reserved_595/Ldl-r_binding_region/1'>low density lipoprotein receptor binding region</scene>, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L). This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE.

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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 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 <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, 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 134-150, 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).  This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE.
+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 <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, 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 134-150, known as the <scene name='Sandbox_Reserved_595/Ldl-r_binding_region/1'>low density lipoprotein receptor binding region</scene>, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L).  This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE.
 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).