Structural complementarity of distance constraints obtained from chemical cross‐linking and amino acid coevolution

Ricardo N Dos Santos, G. F. Bottino, F. Gozzo, F. Morcos, L. Martínez
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引用次数: 3

Abstract

The analysis of amino acid coevolution has emerged as a practical method for protein structural modeling by providing structural contact information from alignments of amino acid sequences. In parallel, chemical cross‐linking/mass spectrometry (XLMS) has gained attention as a universally applicable method for obtaining low‐resolution distance constraints to model the quaternary arrangements of proteins, and more recently even protein tertiary structures. Here, we show that the structural information obtained by XLMS and coevolutionary analysis are effectively complementary: the distance constraints obtained by each method are almost exclusively associated with non‐coincident pairs of residues, and modeling results obtained by the combination of both sets are improved relative to considering the same total number of constraints of a single type. The structural rationale behind the complementarity of the distance constraints is discussed and illustrated for a representative set of proteins with different sizes and folds.
从化学交联和氨基酸共同进化中获得的距离约束的结构互补性
氨基酸协同进化分析已经成为一种实用的蛋白质结构建模方法,通过氨基酸序列比对提供结构接触信息。与此同时,化学交联/质谱法(XLMS)作为一种普遍适用的方法获得低分辨率距离约束,以模拟蛋白质的四级排列,最近甚至是蛋白质三级结构,已经引起了人们的注意。本文表明,XLMS和协同进化分析获得的结构信息是有效互补的:每种方法获得的距离约束几乎都与非重合的残基对相关,并且相对于考虑同一类型的约束总数,两组组合获得的建模结果得到了改进。讨论了距离约束互补性背后的结构原理,并举例说明了具有不同大小和折叠的具有代表性的一组蛋白质。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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