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Effect of the d ‐Phe 2 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)
Author(s) -
Ishida Toshimasa,
In Yasuko,
Inoue Masatoshi,
Yasuda-Kamatani Yoshimi,
Minakata Hiroyuki,
Iwashita Takashi,
Nomoto Kyosuke
Publication year - 1992
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(92)80689-e
Subject(s) - chemistry , residue (chemistry) , stereochemistry , molecule , hydrogen bond , peptide , crystal structure , intermolecular force , crystallography , biochemistry , organic chemistry
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.