Alpha-helix mimicry of a beta-turn.
It is shown here that the three-dimensional arrangement of the amino acids in an RGDF beta-turn (sequence involved in cell adhesion) resembles that of an alpha-helix with a shuffled RGDF sequence (i.e. RGXFD). A miniprotein was designed and constructed which arranges the RGXFD sequence into a well defined helical conformation. The designed protein is bioactive and folds into the desired structure as assessed by nuclear magnetic resonance spectroscopy. The recognition process mediated by a beta-turn can thus be mimicked by an alpha-helix.
CNRS - UPR 9003, Université Louis Pasteur, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, Strasbourg - Illkirch, 67400, France. georges@scripps.edu
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D000595:Amino Acid Sequence; D008958:Models, Molecular; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins; D012604:Scorpion Venoms / Q000737:chemistry
D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D012604:Scorpion Venoms; C084961:arginyl-glycyl-aspartyl-phenylalanine; C056574:leiurotoxin I