作者: Fernando Rodriguez-Pascual , David Anthony Slatter
DOI: 10.1038/SREP37374
关键词: Peptide sequence 、 Mechanical strength 、 Fibril 、 Fibrillar collagen 、 Biochemistry 、 Lysyl oxidase 、 Collagen cross linking 、 Extracellular matrix 、 Biology 、 Phylogenetics
摘要: Collagens constitute a large family of extracellular matrix (ECM) proteins that play fundamental role in supporting the structure various tissues multicellular animals. The mechanical strength fibrillar collagens is highly dependent on formation covalent cross-links between individual fibrils, process initiated by enzymatic action members lysyl oxidase (LOX) family. Fibrillar are present wide variety animals, therefore often being associated with metazoan evolution, where emergence an ancestral collagen chain has been proposed to lead different clades. While LOX-generated cross-linking metabolites have detected families, there limited information about when and how acquired this particular modification. By analyzing telopeptide helical sequences, we identified conserved, potential sites throughout tree life. Based analysis, propose they importantly contributed further expansion collagens.