title: Common topology within a non-collagenous domain of several different collagen types.
abstract: The secondary structure of a conserved non-collagenous module in alpha 1(V), alpha 1(XI), alpha 1(IX), alpha 1(XII), alpha 1(XIV) and alpha 1(XVI) collagen chains and in proline- and arginine-rich protein was analyzed using different algorithms. The results predict that a common anti-parallel beta-sheet structure composed of nine consensus beta-strands is present in these non-collagenous modules. A model for the packing of these beta-sheets is proposed which suggests that the predicted beta-sheet structure may be involved in molecular recognition functions.
authors.affiliation: Institut de Biologie et de Chimie des Protéines, UPR412-CNRS, Lyon, France.
authors.forename: M
authors.initials: M
authors.lastname: Moradi-Améli
authors.forename: G
authors.initials: G
authors.lastname: Deléage
authors.forename: C
authors.initials: C
authors.lastname: Geourjon
authors.forename: M
authors.initials: M
authors.lastname: van der Rest
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000235:genetics; D016384:Consensus Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
chemical_list: D003094:Collagen