![]() AnaC Calvo, Laura Moreno, Leticia Moreno, JanneM Toivonen, Raquel Manzano, Nora Molina, Miriam de la Torre, Tresa López, FranciscoJ Miana-Mena, MaríaJ Muñoz, Pilar Zaragoza, Pilar Larrodé, Alberto García-Redondo, Rosario Osta.Complexities of the glomerular basement membrane. Physical Chemistry Chemical Physics 2022, 24 The effects of glycine to alanine mutations on the structure of GPO collagen model peptides. These findings will shed light on how the interruption sequence influences the conformation of the collagen molecule and provide a structural basis for further functional studies. ![]() Our results, for the first time, also identified the binding of zinc to the end of the triple helix. In addition, our structures provide a detailed view of the dynamic property of such an interrupted zone with respect to hydrogen bonding topology, torsion angles, and helical parameters. These could partly explain the difference in thermal stability between the different interruptions. Furthermore, at the G5G interruption site, the presence of Ala and Leu residues, both with free N–H groups, allows the formation of more direct and water-mediated interchain hydrogen bonds than in the related Gly → Ala structure. In these structures, the interruption zone brings localized disruptions to the triple helix and introduces a light 6–8° bend with the same directional preference to the whole molecule, which may correspond structurally to the first physiological kink site in type XIX collagen. We determined the crystal structures of the host–guest peptide (GPO) 3-GPOALO-(GPO) 4 to 1.03 Å resolution in two crystal forms. Here, we focused on a G5G type natural interruption sequence G-POALO-G from human type XIX collagen, a homotrimer collagen, as this sequence possesses distinct properties compared with those of a pathological similar Gly mutation sequence in collagen mimic peptides. The structural feature of the interruption sequences and the molecular basis for their functions have not been well studied. Naturally occurring interruptions in nonfibrillar collagen play key roles in molecular flexibility, collagen degradation, and ligand binding.
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