Molecular conformation of achatin‐I, an endogenous neuropeptide containing D‐amino acid residue
Authors:
- 10 December 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 276 (1-2) , 95-97
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' β‐turn structure with the D‐Phe‐Ala residues at the corner of the bend, which is further stabilized by two NH(Gly)βCγ=Oδ(Asp) and NH(Asp)βCγ=Oδ(Asp) intramolecular hydrogen bonds. This turn conformation may be an important feature of achatin‐I related to its neuroexcitatory activity.Keywords
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