The NC2 domain of type IX collagen determines the chain register of the triple helix.

ABSTRACT: Precise mapping and unraveling the mechanism of interaction or degradation of a certain type of collagen triple helix requires the generation of short and stable collagenous fragments. This is a great challenge especially for hetero-trimeric collagens, where chain composition and register (stagger) are important factors. No system has been reported that can be efficiently used to generate a natural collagenous fragment with exact chain composition and desired chain register. The NC2 domain (only 35-50 residues) of FACIT collagens is a potent trimerization domain. In the case of type IX collagen it provides the efficient selection and hetero-trimerization of three distinct chains. The ability of the NC2 domain to determine the chain register of the triple helix is studied. We generated thre

SUBMITTER: Boudko SP 

PROVIDER: S-EPMC3531767 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature