LOX-1 (lectin-like oxidized low-density lipoprotein receptor 1) is the major oxidized LDL (OxLDL) receptor on endothelial cells. The extracellular part of LOX-1 comprises an 82-residue stalk region (NECK) and a C-type lectin-like ligand-binding domain (CTLD). The NECK displays sequence similarity to the coiled-coil region of myosin, having been suggested it adopts a rod-like structure. In this article, we report the structural analyses of human LOX-1 NECK using a variety of approaches including limited proteolysis, chemical cross-linking, circular dichroism (CD) and NMR. Our analysis reveals a unique structural feature of the LOX-1 NECK. Despite significant sequence similarity with the myosin coiled-coil, LOX-1 NECK does not form a uniform rod-like structure. Although not random, one-third of the N-terminal NECK is less structured than the remainder of the protein and is highly sensitive to cleavage by a variety of proteases. The coiled-coil structure is localized at the C-terminal part of the NECK, but is in dynamic equilibrium among multiple conformational states on a mus-ms time scale. This chimeric structural property of the NECK region may enable clustered LOX-1 on the cell surface to recognize OxLDL.