Relating three-dimensional structures to protein networks provides evolutionary insights

Relating three-dimensional structures to protein networks provides evolutionary insights
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DOI:
10.1126/science.1136174
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发表时间:
2006-12-22
期刊:
影响因子:
56.9
通讯作者:
Gerstein, Mark B.
Gerstein, Mark B.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Kim, Philip M.;Lu, Long J.;Gerstein, Mark B.

文献摘要

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大多数蛋白质网络的研究都在高度抽象的层面上进行,忽略了每种相互作用的结构和化学方面。在此,我们利用来自三维蛋白质结构的原子分辨率信息来描述相互作用的特征。我们发现,网络拓扑结构和基因组特征之间一些先前已被认识到的关系(例如,枢纽蛋白往往是必需蛋白质)实际上更多地反映了一种结构量,即不同结合界面的数量。根据这一数量对枢纽蛋白进行细分,可以深入了解它们的进化速率,并表明网络增长的其他机制在进化中是活跃的(除了通过基因复制产生的有效优先连接之外)。
Most studies of protein networks operate on a high level of abstraction, neglecting structural and chemical aspects of each interaction. Here, we characterize interactions by using atomic-resolution information from three-dimensional protein structures. We find that some previously recognized relationships between network topology and genomic features ( e. g., hubs tending to be essential proteins) are actually more reflective of a structural quantity, the number of distinct binding interfaces. Subdividing hubs with respect to this quantity provides insight into their evolutionary rate and indicates that additional mechanisms of network growth are active in evolution ( beyond effective preferential attachment through gene duplication).