蛋白质-蛋白质相互作用的结构特征和演化。

Joachim Von Eichborn, Stefan Günther, Robert Preissner
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引用次数: 0

摘要

蛋白质复合物结构的解决为蛋白质功能和分子识别提供了基本的见解。虽然测定蛋白质-蛋白质复合物通常比测定单个蛋白质更困难,但在过去十年中,实验测定的复合物的数量显著增加。本文分析了750个瞬时蛋白质-蛋白质相互作用的界面以及同一蛋白质链结构域之间的2000个相互作用(专性相互作用),以更好地了解分子识别并确定适用于蛋白质结合位点预测的特征。基于知识的电位计算表明,具有互补物理化学性质的氨基酸之间的接触是优先的。整个界面区域的氨基酸守恒分析表明,与永久暴露于溶剂的表面区域相比,蛋白质结合位点的进化守恒倾向较弱但显著。值得注意的是,非常保守的残基之间的接触频率比预期的要高得多,这证实了所谓的“热点”理论。专性结构域与瞬态结构域接触的比较揭示了蛋白质相互作用的差异,并指出蛋白质相互作用的结构多样化和分子识别受到其他进化方面的影响,而不是专性结构域与域相互作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structural features and evolution of protein-protein interactions.

Solved structures of protein-protein complexes give fundamental insights into protein function and molecular recognition. Although the determination of protein-protein complexes is generally more difficult than solving individual proteins, the number of experimentally determined complexes increased conspicuously during the last decade. Here, the interfaces of 750 transient protein-protein interactions as well as 2,000 interactions between domains of the same protein chain (obligate interactions) were analyzed to obtain a better understanding of molecular recognition and to identify features applicable for protein binding site prediction. Calculation of knowledge-based potentials showed a preference of contacts between amino acids having complementary physicochemical properties. The analysis of amino acid conservation of the entire interface area showed a weak but significant tendency to a higher evolutionary conservation of protein binding sites compared to surface areas that are permanently exposed to solvent. Remarkably, contact frequencies between outstandingly conserved residues are much higher than expected confirming the so-called "hot spot" theory. The comparisons between obligate and transient domain contacts reveal differences and point out that structural diversification and molecular recognition of protein-protein interactions are subjected to other evolutionary aspects than obligate domain-domain interactions.

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