The collagen superfamily is highly complex and shows a remarkable diversity in molecular and supramolecular organization, tissue distribution and function. However, all its members share a common structural feature, the presence of at least one triple-helical domain, which corresponds to a number of (Gly-X-Y)n repeats (X being frequently proline and Y hydroxyproline) in the amino acid sequence. Several sub-families have been determined according to sequence homologies and to similarities in the structural organization and supramolecular assembly. In the present review, we focus on the newly described fibrillar collagens, fibrillar-associated collagens with interrupted triple helix, membrane collagens and multiplexins. Recent advances in the characterization of proteins containing triple-helical domains but not referred to as collagens are also discussed.