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首页> 外文期刊>Biochemistry >Do the structures of big ET-1 and big ET-3 adopt a similar overall fold? Consequences for endothelin converting enzyme specificity.
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Do the structures of big ET-1 and big ET-3 adopt a similar overall fold? Consequences for endothelin converting enzyme specificity.

机译：大ET-1和大ET-3的结构是否采用相似的整体折叠率？内皮素转化酶特异性的后果。

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摘要

Big ET-1 and big ET-3 are precursor peptides which render endothelin-1 (ET-1) and endothelin-3 (ET-3) relatively unreactive and resistant to proteolytic cleavage. Big ET-1 is cleaved in vivo by ECE-1 (endothelin-converting enzyme), and big ET-3 is also cleaved but apparently to a significantly lesser extent by this enzyme. To shed light on the relation between structure and function, circular dichroism (CD) spectroscopy and homology modeling were used to determine whether big ET-1 and big ET-3 adopt similar secondary and tertiary structures. Analyses of the CD spectra and thermal denaturation indicate they have similar secondary structures and thermal stabilities. Superposition of the modeled coordinates of both peptides indicates that they can adopt the same overall fold except in the C-terminal residues, 34-38 in big ET-1 and 34-41 in big ET-3. This region corresponds to an area of complete sequence heterogeneity between the two peptides. A model has been developed which has a loop for residues 27-30 (HVVP in big ET-1), which have previously been demonstrated to be essential for eliciting efficient hydrolysis of the W21-V22 bond in big ET-1 and which have the sequence QTVP in big ET-3. Differences in affinity between big ET-1 and big ET-3 for ECE-1 thus appear to be due solely to sequence variations in the local region of the cleavage site.
机译：大ET-1和大ET-3是前体肽，可使内皮素1（ET-1）和内皮素3（ET-3）相对无反应，并且对蛋白水解裂解具有抵抗力。大ET-1在体内被ECE-1（内皮素转化酶）裂解，大ET-3也被裂解，但显然被该酶裂解的程度要小得多。为了阐明结构与功能之间的关系，使用圆二色性（CD）光谱和同源性模型确定大ET-1和大ET-3是否采用相似的二级和三级结构。 CD光谱和热变性的分析表明它们具有相似的二级结构和热稳定性。两种肽的建模坐标的叠加表明，除了C端残基（大ET-1中的34-38和大ET-3中的34-41）外，它们可以采用相同的总体折叠。该区域对应于两个肽之间完全序列异质性的区域。已开发出一种模型，该模型具有一个残基27-30（大ET-1中的HVVP）的环，先前已证明这对于引发大ET-1中W21-V22键的有效水解至关重要，并且具有在大型ET-3中对QTVP进行排序。因此，大的ET-1和大的ET-3对ECE-1的亲和力差异似乎完全是由于切割位点局部区域的序列变异所致。

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