title: Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form.
abstract: The molecular conformation of achatin-I neutral form (H-Gly-D-Phe-Ala-Asp-OH), an endogenous neuropeptide, was elucidated by X-ray crystal analysis. The molecule has a type II' beta-turn structure with the D-Phe-Ala residues at the corner of the bend, which is further stabilized by two NH(Gly)...C gamma = O sigma(Asp) and NH(Asp)...C gamma = O sigma(Asp) intramolecular hydrogen bonds. This turn conformation may be an important feature of achatin-I related to its neuroexcitatory activity.
authors.affiliation: Suntory Institute for Bioorganic Research, Osaka, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kamatani
authors.forename: H
authors.initials: H
authors.lastname: Minakata
authors.forename: T
authors.initials: T
authors.lastname: Iwashita
authors.forename: K
authors.initials: K
authors.lastname: Nomoto
authors.forename: Y
authors.initials: Y
authors.lastname: In
authors.forename: M
authors.initials: M
authors.lastname: Doi
authors.forename: T
authors.initials: T
authors.lastname: Ishida
mesh_terms: D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification; D018377:Neurotransmitter Agents / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D009479:Neuropeptides; D018377:Neurotransmitter Agents; C059927:achatin I