title: Effect of the D-Phe2 residue on molecular conformation of an endogenous neuropeptide achatin-I. Comparison of X-ray crystal structures of achatin-I (H-Gly-D-Phe-Ala-Asp-OH) and achatin-II (H-Gly-Phe-Ala-Asp-OH).
abstract: The molecular conformation of achatin-II neutral form (H-Gly-Phe-Ala-Asp-OH), an endogenous peptide from the Achatina fulica ganglia, was elucidated by X-ray crystal analysis. The molecule takes an extended beta-pleated structure stabilized by 5 intermolecular hydrogen bonds with the antiparallely arranged molecules. This is in contrast with the turn conformation of a neuroactive achatin-I (H-Gly-D-Phe-Ala-Asp-OH) [(1992) FEBS Lett. 276,95-97]. The conformational comparison of both of the molecules makes clear the structural role which D-Phe residue of achatin-I plays in forming a definite active form.
authors.affiliation: Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Ishida
authors.forename: Y
authors.initials: Y
authors.lastname: In
authors.forename: M
authors.initials: M
authors.lastname: Inoue
authors.forename: Y
authors.initials: Y
authors.lastname: Yasuda-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
mesh_terms: D000595:Amino Acid Sequence; D007447:Invertebrate Hormones / Q000737:chemistry*; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D007447:Invertebrate Hormones; D009479:Neuropeptides; C059927:achatin I; D010649:Phenylalanine