Sandbox Reserved 595: Difference between revisions

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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).

Connecting the N-terminal and C-terminal domains is the flexible hinge region, which extends approximately from residue 165 to residue 215 (B,H). This region is protease sensitive (M).

ApoE exhibits extensive domain interactions. Hydrogen bonds and salt-bridges act to shield the major LDLR-binding region. This protein's unique topology regulates its tertiary structure in order to solely permit one conformation upon binding in a two-step manner. Lipid-free and partially lipidated ApoE are thwarted from prematurely binding to ApoE receptors by the tertiary structure. Therefore, the optimal receptor-binding affinity of fully lipidated ApoE is guaranteed. An active conformation for biding to members of the low-density lipoprotein receptor family is achieved through binding to lipids and HSPGs (V).

Sandbox Reserved 595: Difference between revisions

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 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).
+Connecting the N-terminal and C-terminal domains is the flexible hinge region, which extends approximately from residue 165 to residue 215 (B,H).  This region is protease sensitive (M).
+ApoE exhibits extensive domain interactions.  Hydrogen bonds and salt-bridges act to shield the major LDLR-binding region.  This protein's unique topology regulates its tertiary structure in order to solely permit one conformation upon binding in a two-step manner.  Lipid-free and partially lipidated ApoE are thwarted from prematurely binding to ApoE receptors by the tertiary structure.  Therefore, the optimal receptor-binding affinity of fully lipidated ApoE is guaranteed.  An active conformation for  biding to members of the low-density lipoprotein receptor family is achieved through binding to lipids and HSPGs (V).