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• W2002022989 abstract "The high-resolution NMR structure of apolipophorin III from the sphinx moth, Manduca sexta, has been determined in the lipid-free state. We show that lipid-free apolipophorin III adopts a unique helix-bundle topology that has several characteristic structural features. These include a marginally stable, up-and-down helix bundle that allows for concerted opening of the bundle about hinged loops upon lipid interaction and buried polar/ionizable residues and buried interhelical H-bonds located in the otherwise hydrophobic interior of the bundle that adjust protein stability and facilitate lipid-induced conformational opening. We suggest that these structural features modulate the conformational adaptability of the lipid-free helix bundle upon lipid binding and control return of the open conformation to the original lipid-free helix-bundle state. Taken together, these data provide a structural rationale for the ability of exchangeable apolipoproteins to reversibly interact with circulating lipoprotein particles." @default.
• W2002022989 created "2016-06-24" @default.
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• W2002022989 date "2002-01-29" @default.
• W2002022989 modified "2023-10-18" @default.
• W2002022989 title "Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein" @default.
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• W2002022989 doi "https://doi.org/10.1073/pnas.032565999" @default.
• W2002022989 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/122165" @default.
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