Versican is a member of the chondroitin sulphate (CS) proteoglycan family, which also includes versican/PG-M, aggrecan, neurocan and brevican. These proteoglycans are characterized by the presence of a hyaluronan-binding domain and a C-type lectin domain in their core proteins. Through these domains, lecticans interact with carbohydrate and protein ligands in the extracellular matrix and act as linkers of these extracellular matrix molecules. See: Cell Mol Life Sci 2000 Feb;57(2):276-89 A proteoglycan core peptide. Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican. See: J Biol Chem 1999 Jul 16;274(29):20444-9
Aggrecan, versican, neurocan, and brevican are important components of the extracellular matrix in various tissues. Their amino-terminal globular domains bind to hyaluronan, but the function of their carboxyl-terminal globular domains has long remained elusive. aggrecan, versican, and brevican lectin domains bind fibulin-2, whereas neurocan does not. As expected for a C-type lectin, the interactions are calcium-dependent, with K(D) values in the nanomolar range as measured by surface plasmon resonance.