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Model of apoLp-III binding interaction (not to scale). In the lipid-free state, apoLp-III exists as a closed five-helix bundle, poised to bind to lipophorin. Appearance of DAG in the lipoprotein surface monolayer induces apoLp-III binding at its helix 3′ end, which triggers helix-bundle opening. This opening ultimately leads to replacement of helix–helix contacts in the bundle conformation by helix–lipid contacts in the lipoprotein-bound state.
