Effect of the D-Phe2 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).
FEBS Lett
; 307(3): 253-6, 1992 Aug 03.
Article
en En
| MEDLINE
| ID: mdl-1644179
ABSTRACT
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 beta-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.
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Banco de datos:
MEDLINE
Asunto principal:
Fenilalanina
/
Neuropéptidos
/
Hormonas de Invertebrados
Idioma:
En
Año:
1992
Tipo del documento:
Article