Identification of the second cluster of ligand-binding repeats in megalin as a site for receptor-ligand interactions

摘要

Megalin is a large cell surface receptor that mediates the binding and internalization of a number of structurally and functionally distinct ligands from the li- poprotein and protease:protease inhibitor families. To begin to address how megalin is able to bind ligands with unique structurally properties, we have mapped a binding site for apolipoprotein E (apoE)-β very low density lipoprotein (βVLDL), lipoprotein lipase, aprotinin, lactoferrin, and the receptor-associated protein (RAP) within the primary se- quence of the receptor. RAP is known to inhibit the binding of all ligands to megalin.