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