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)

FEBS Letters

Iwashita, Takashi¹  Minakata, Hiroyuki¹  In, Yasuko²  Inoue, Masatoshi²  Ishida, Toshimasa²  Nomoto, Kyosuke¹  Yasuda-Kamatani, Yoshimi¹ 

[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;    Achatin-II;    Neuropeptide;    Molecular conformation;    Crystal structure;   

DOI  :  10.1016/0014-5793(92)80689-E

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-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 β-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.

【 授权许可】

Unknown