MOLECULAR-CONFORMATION OF ACHATIN-I, AN ENDOGENOUS NEUROPEPTIDE CONTAINING D-AMINO-ACID RESIDUE - X-RAY CRYSTAL-STRUCTURE OF ITS NEUTRAL FORM

被引：20

作者：

KAMATANI, Y

MINAKATA, H

IWASHITA, T

NOMOTO, K

IN, Y

DOI, M

ISHIDA, T

机构：

[1] OSAKA UNIV PHARMACEUT SCI,DEPT PHYS CHEM,2-10-65 KAWAI,MATSUBARA,OSAKA 580,JAPAN

[2] SUNTORY INST BIOORGAN RES,SHIMAMOTO,OSAKA 618,JAPAN

来源：

FEBS LETTERS | 1990年 / 276卷 / 1-2期

关键词：

ACHATIN-I; NEUROTRANSMITTER; TETRAPEPTIDE; MOLECULAR CONFORMATION; CRYSTAL STRUCTURE;

D O I：

10.1016/0014-5793(90)80516-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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' 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-delta(Asp) and NH(Asp)...C-gamma=O-delta(Asp) intramolecular hydrogen bonds. This turn conformation may be an important feature of achatin-I related to its neuroexcitatory activity.

引用

页码：95 / 97

页数：3

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