Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form.
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.
Kamatani
Y
Y
Suntory Institute for Bioorganic Research, Osaka, Japan.
Minakata
H
H
Iwashita
T
T
Nomoto
K
K
In
Y
Y
Doi
M
M
Ishida
T
T
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
D009479:Neuropeptides; D018377:Neurotransmitter Agents; C059927:achatin I