{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["287(53)"],"submitter":["Boudko SP"],"pubmed_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"],"journal":["The Journal of biological chemistry"],"pagination":["44536-45"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3531767"],"repository":["biostudies-literature"],"pubmed_title":["The NC2 domain of type IX collagen determines the chain register of the triple helix."],"pmcid":["PMC3531767"],"pubmed_authors":["Boudko SP","Bachinger HP"],"additional_accession":[]},"is_claimable":false,"name":"The NC2 domain of type IX collagen determines the chain register of the triple helix.","description":"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","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Dec","modification":"2025-04-04T21:16:36.725Z","creation":"2019-03-27T01:02:16Z"},"accession":"S-EPMC3531767","cross_references":{"pubmed":["23132862"],"doi":["10.1074/jbc.m112.417543","10.1074/jbc.M112.417543"]}}