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Article

Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization.

Journal of molecular biology - 9 Aug 2002

Sahoo Daisy, Weers Paul M M, Ryan Robert O, Narayanaswami Vasanthy

Abstract excerpt

Apolipophorin III (ApoLp-III) from the Sphinx moth, Manduca sexta, is an 18kDa protein that binds reversibly to hydrophobic surfaces generated on metabolizing lipoprotein particles. It is comprised of amphipathic alpha-helices (H1-H5) organized in an up-and-down topology forming a helix bundle in the lipid-free state. Upon interaction with lipids, apoLp-III has been proposed to undergo a dramatic conformational...

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Identifiers

PMID: 12144779
DOI: 10.1016/s0022-2836(02)00618-6

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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