Abstract
Cartilage matrix protein (CMP) is a noncollagenous glycoprotein with a molecular mass of 148 kDa consisting of three identical subunits linked together at their C-terminal assembly domains via a coiled-coil α-helix (Hauser and Paulsson 1994). Electron microscopy of the native protein showed trimers with compact ellipsoid subunits, each consisting of two von Willebrand factor A-domains linked via one EGF-like repeat. CMP is a highly insoluble protein which appears to become covalently crosslinked within the cartilage matrix with maturation.