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. Author manuscript; available in PMC: 2013 Aug 7.
Published in final edited form as: Biochemistry. 2012 Jul 25;51(31):6220–6227. doi: 10.1021/bi300619a

Figure 7.

Figure 7

Proposed model of the binding of apoLp-III to LPS. ApoLp-III first associates superficially to the LPS carbohydrates which protrude into the aqueous environment. Penetration into the interior of the LPS micelles provide access to the hydrophobic Lipid A region, which is then followed by LPS disaggregation. A conformational change of the protein allows direct interaction of the hydrophobic protein interior with the lipid A region, leading to the formation of a stable apoLp-III/LPS complex. The resulting product is an assembly of 4 apoLp-III and 24 LPS molecules with a size of ~ 400 kDa.