Signal Epitopes in the Three‐Dimensional Structure of Neuropeptide Y

Signal Epitopes in the Three‐Dimensional Structure of Neuropeptide Y
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神经肽Y三维结构中的信号表位

DOI:
10.1111/j.1749-6632.1990.tb48920.x
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发表时间:
1990
影响因子:
5.2
通讯作者:
Berith Bjørnholm
Berith Bjørnholm
中科院分区:
综合性期刊3区
文献类型:
--
作者:
T. Schwartz;J. Fuhlendorff;L. Kjems;METTE S. Kristensen;Mees Vervelde;M. O'Hare;J. Krstenansky;Berith Bjørnholm

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通常理解,调节肽被其靶细胞上的受体识别为三维结构。然而,我们对生物活性肽的结构和功能之间的关系的真实的知识在很大程度上限于关于其一级结构的某些部分的重要性的一些信息。虽然晶体结构可用于一些肽,例如胰高血糖素,但这些结构与肽的生物活性构象的相关性尚不清楚,因为大多数肽在水溶液中不具有明确的结构。然而,这些肽中的一些已被核磁共振(NMR)显示折叠成有序的构象时,水的活性降低有机溶剂或在脂质胶束的存在下。这些“人工”溶液结构是否与肽的受体结合构象相关是一个有趣的可能性,但仍然只是猜测。神经肽Y(NPY)、肽YY(PYY)和胰多肽(PP)是所谓的PP折叠肽家族的成员,其不同于大多数其他小分子多肽。
It is generally appreciated that regulatory peptides are recognized as three-dimensional structures by the receptors on their target cells. However, our real knowledge of the relationship between the structure and the function of biologically active peptides to a large degree is limited to some information on the importance of certain parts of their primary structure. Although crystal structures are available for a few peptides, for example glucagon, the relevance of these structures for the biologically active conformation of the peptide is unclear because most peptides do not hold a well-defined structure in aqueous solution. Nevertheless, some of these peptides have been shown by nuclear magnetic resonance (NMR) to fold into ordered conformations when the water activity is decreased by organic solvents or in the presence of lipid micelles. Whether these ‘artificial’ solution structures are of relevance for the receptor-binding conformation of the peptides is an interesting possibility but is still only speculation. Neuropeptide Y (NPY), peptide YY (PYY), and pancreatic polypeptide (PP) are members of the so-called PP-fold family of peptides, which differ from most other small
通过模型肽的设计、合成和研究,检查 β-内啡肽中两亲性螺旋结构的需求。
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