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首页> 外文期刊>Journal of Molecular Biology >DEAMIDATION IN PROTEINS - THE CRYSTAL STRUCTURE OF BOVINE PANCREATIC RIBONUCLEASE WITH AN ISOASPARTYL RESIDUE AT POSITION 67
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DEAMIDATION IN PROTEINS - THE CRYSTAL STRUCTURE OF BOVINE PANCREATIC RIBONUCLEASE WITH AN ISOASPARTYL RESIDUE AT POSITION 67

机译：蛋白质中的脱氨作用-带有67位异戊二烯残基的牛胰腺核糖核酸酶的晶体结构

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摘要

The non-enzymatic deamidation of asparagine residues in proteins is a widely occurring reaction, both in vivo and in vitro. Although the importance of this process is commonly recognised, only little structural information is available on it. In order to evaluate the structural effects of this reaction in proteins, we have determined the crystal structure of a ribonuclease A derivative in which asparagine 67 has been replaced by an isoaspartyl residue, as a consequence of an in vitro deamidation reaction. The overall structure of the model, refined to a crystallographic R-factor of 0.159 at a resolution of 1.9 Angstrom, is very similar to that of the native protein, but considerable deviations are observed in the region delimited by the disulphide bridge 65-72. In particular, the insertion of an extra methylene group in the main chain at residue 67 breaks up the hydrogen bond network that makes this region rater rigid in ribonuclease Angstrom. On the basis of the structure observed, some of the slightly but significantly different properties of this deamidated derivative, with respect to the native enzyme, can be explained. (C) 1996 Academic Press Limited [References: 26]
机译：蛋白质中天冬酰胺残基的非酶脱酰胺作用是体内和体外广泛发生的反应。尽管通常认识到此过程的重要性，但关于它的结构信息很少。为了评估该反应在蛋白质中的结构效果，我们确定了核糖核酸酶A衍生物的晶体结构，该衍生物中的天冬酰胺67已被异天冬酰胺残基取代，这是体外脱酰胺化反应的结果。该模型的整体结构以1.9埃的分辨率精炼到0.159的晶体学R因子，与天然蛋白质非常相似，但是在由二硫键65-72界定的区域中观察到了相当大的偏差。特别地，在主链上的残基67处插入一个额外的亚甲基会破坏氢键网络，从而使该区域评估者在核糖核酸酶埃中呈刚性。基于观察到的结构，可以解释该脱酰胺化衍生物相对于天然酶的一些稍微但明显不同的性质。 （C）1996 Academic Press Limited [参考号：26]

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