Sandbox Reserved 595: Difference between revisions
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lipoproteins. J. Biol. Chem.271:19053–19057.</ref>'. This region is protease sensitive '<ref>Freiden, Carl and K. Garai. 2012. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease. PNAS 109(23):8913-8919.</ref>'. | lipoproteins. J. Biol. Chem.271:19053–19057.</ref>'. This region is protease sensitive '<ref>Freiden, Carl and K. Garai. 2012. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease. PNAS 109(23):8913-8919.</ref>'. | ||
[[Image:ApoE_Sandbox_Reserved_595.jpg]] | [[Image:ApoE_Sandbox_Reserved_595.jpg|thumb|left|350px]] | ||
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 '<ref>Chen, J et al. 2011. Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions. Proc Natl Acad Sci USA 108(36):14813-8.</ref>'. | 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 '<ref>Chen, J et al. 2011. Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions. Proc Natl Acad Sci USA 108(36):14813-8.</ref>'. | ||