Molecular conformation of achatin‐I, an endogenous neuropeptide containing D‐amino acid residue

FEBS Letters

Kamatani, Yoshimi¹  Doi, Mitsunobu²  Iwashita, Takashi¹  Minakata, Hiroyuki¹  In, Yasuko²  Ishida, Toshimasa²  Nomoto, Kyosuke¹ 

[1] Suntory Institute for Bioorganic Research, Shimamoto-cho, Mishima-gun, Osaka 618 Japan;Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara, Osaka 580, Japan

关键词: Achatin-I;    Neurotransmitter;    Tetrapeptide;    Molecular conformation;    Crystal structure;   

DOI  :  10.1016/0014-5793(90)80516-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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' β-turn structure with the D-Phe-Ala residues at the corner of the bend, which is further stabilized by two NH(Gly)βC^γ=O^δ(Asp) and NH(Asp)βC^γ=O^δ(Asp) intramolecular hydrogen bonds. This turn conformation may be an important feature of achatin-I related to its neuroexcitatory activity.

【 授权许可】

Unknown