Schematic overview. Plasma purified β2GPI in its closed conformation does not bind to the LRP receptor. (1) On interaction of LPS with domain V of β₂GPI, (2) A conformational change occurs in β₂GPI. The “active” fishhook-like conformation of β₂GPI in complex with LPS is then able to bind to the receptor (3) after which the β₂GPI-LPS complex is cleared. (4) The scavenging of LPS by β₂GPI leads to a decreased binding of LPS to the TLR4 receptor (5), resulting in a decreased expression of the inflammatory markers TNF-α, IL-6, and IL-8. (6)