Mechanisms of collagen trimer assembly

Abstract

It is generally accepted that the folding of collagen triple helical domains occur from the C-terminus toward the N-terminus by a zipper mechanism. The regions at the C-terminus of the triple helices must therefore play a critical role in the processes of chain recognition and assembly to get the proper stoichiometries and of chain registration to align the chains for the folding of the triple helix. Examination of these regions reveals a broad diversity of structures and suggests that different mechanisms of assembly are used in the various collagen and collagen-like molecules. We review here three different mechanisms that have recently come to light. The collectins, a group of serum proteins containing collagen-like triple helical domains, are assembled through hydrophobic interactions in a triple a helix. Collagens VIII and X, Clq and several related proteins contain homologous C-terminal domains that are characterized by a -pleated sheet structure. They assemble through very strong hydrophobic interactions that probably involve an aromatic zipper. Collagens IX, XII and XIV fibril associated collagen with interrupted triple helices (FACITs), are assembled by a mechanism in which both the C-terminal triple helix and a very short cysteine-containing sequence are involved. © Indian Academy of Sciences.