Premium
Molecular conformation of achatin‐I, an endogenous neuropeptide containing D‐amino acid residue
Author(s) -
Kamatani Yoshimi,
Minakata Hiroyuki,
Iwashita Takashi,
Nomoto Kyosuke,
In Yasuko,
Doi Mitsunobu,
Ishida Toshimasa
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80516-l
Subject(s) - residue (chemistry) , chemistry , endogeny , amino acid residue , neuropeptide , biochemistry , amino acid , stereochemistry , peptide sequence , receptor , gene
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.