Wang Z, Orchard I, Lange A B, Chen X
Department of Zoology, University of Toronto, Ontario, Canada.
Neuropeptides. 1995 May;28(5):261-6. doi: 10.1016/0143-4179(95)90042-x.
In the oviduct of Locusta migratoria, a FMRFamide-related peptide, PDVDHVFLRFamide (SchistoFLRFamide) acts as a neuromodulator, inhibiting spontaneous and induced muscle contraction. In this study, we have used N-terminal truncated peptides to show that PDVDHVFLRFamide has separated binding and activation regions. VFLRFamide is the minimum sequence required for binding, whereas HVFLRFamide is the minimum sequence for inhibitory biological activity. Thus the His residue, which does not contribute to binding, is a critical amino acid for the activation of the receptor. The N-terminal PDVD appears to play little or no role in either binding or activation. VFLRFamide, which binds to the receptor but yields no inhibitory biological activity, is a strong antagonist of PDVDHVFLRFamide.
在飞蝗的输卵管中，一种与FMRF酰胺相关的肽，PDVDHVFLRF酰胺（血吸虫FLRF酰胺）作为一种神经调质，抑制自发的和诱导的肌肉收缩。在本研究中，我们使用N端截短的肽来表明PDVDHVFLRF酰胺具有分离的结合区和激活区。VFLRF酰胺是结合所需的最小序列，而HVFLRF酰胺是抑制性生物活性所需的最小序列。因此，对结合无贡献的组氨酸残基是受体激活的关键氨基酸。N端的PDVD在结合或激活中似乎几乎不起作用或不起作用。与受体结合但不产生抑制性生物活性的VFLRF酰胺是PDVDHVFLRF酰胺的强拮抗剂。
