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首页> 外文期刊>Journal of Molecular Biology >Solution Structure of the Pro-hormone Convertase 1 Pro-domain from Mus musculus.
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Solution Structure of the Pro-hormone Convertase 1 Pro-domain from Mus musculus.

机译：小家鼠促激素转化酶1促结构域的溶液结构。

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The solution structure of the mouse pro-hormone convertase (PC) 1 pro-domain was determined using heteronuclear NMR spectroscopy and is the first structure to be obtained for any of the domains in the convertase family. The ensemble of NMR-derived structures shows a well-ordered core consisting of a four-stranded antiparallel beta-sheet with two alpha-helices packed against one side of this sheet. Sequence homology suggests that the other eukaryotic PC pro-domains will have the same overall fold and most of the residues forming the hydrophobic core of PC1 are highly conserved within the PC family. However, some of the core residues are predicted by homology to be replaced by polar amino acid residues in other PC pro-domains and this may help to explain their marginal stability. Interestingly, the folding topology observed here is also seen for the pro-domain of bacterial subtilisin despite little or no sequence homology. Both the prokaryotic and eukaryotic structures have hydrophobic residues clustered on the solvent-accessible surface of their beta-sheets although the individual residue types differ. In the bacterial case this region is buried at the binding interface with the catalytic domain and, in the eukaryotic PC family, these surface residues are conserved. We therefore propose that the hydrophobic patch in the PC1 pro-domain is involved in the binding interface with its cognate catalytic domain in a similar manner to that seen for the bacterial system. The PC1 pro-domain structure also reveals potential mechanisms for the acid-induced dissociation of the complex between pro- and catalytic domains. (c) 2002 Elsevier Science Ltd.
机译：小鼠原激素转化酶（PC）1前域的溶液结构是使用异核NMR光谱确定的，并且是转化酶家族中任何域的第一个结构。 NMR衍生结构的整体显示出一个井井有条的核心，该核心由四链反平行β-折叠组成，两个α-螺旋堆积在该折叠纸的一侧。序列同源性表明，其他真核PC前结构域将具有相同的整体折叠，并且形成PC1疏水核心的大多数残基在PC家族中高度保守。然而，通过同源性预测某些核心残基将被其他PC前域中的极性氨基酸残基取代，这可能有助于解释其边缘稳定性。有趣的是，尽管几乎没有或没有序列同源性，但在细菌枯草蛋白酶的前域也观察到了这里观察到的折叠拓扑。尽管各个残基类型不同，但原核和真核结构均具有聚集在其β折叠的溶剂可及表面上的疏水残基。在细菌的情况下，该区域被掩埋在与催化结构域的结合界面处，在真核PC家族中，这些表面残基是保守的。因此，我们建议以类似于细菌系统所见的方式，将PC1前域中的疏水性补丁与其与其关联的催化域结合到结合界面中。 PC1前结构域结构还揭示了前结构域和催化结构域之间酸诱导的复合物解离的潜在机制。 （c）2002爱思唯尔科学有限公司。

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