Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form.
作者信息
Kamatani Y, Minakata H, Iwashita T, Nomoto K, In Y, Doi M, Ishida T
机构信息
Suntory Institute for Bioorganic Research, Osaka, Japan.
出版信息
FEBS Lett. 1990 Dec 10;276(1-2):95-7. doi: 10.1016/0014-5793(90)80516-l.
PMID:1979949
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.
摘要
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Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form.
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