A METHOD TO PREDICT FUNCTIONAL RESIDUES IN PROTEINS

A METHOD TO PREDICT FUNCTIONAL RESIDUES IN PROTEINS
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DOI:
10.1038/nsb0295-171
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发表时间:
1995-02-01
期刊:
NATURE STRUCTURAL BIOLOGY
影响因子:
--
通讯作者:
VALENCIA, A
VALENCIA, A
中科院分区:
其他
文献类型:
--
作者:
CASARI, G;SANDER, C;VALENCIA, A

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蛋白质的生物活性通常取决于少量功能残基的存在。单独从氨基酸序列鉴定这些残基将是有用的。传统上,预测严格保守的残基是功能性的,但通常保守模式更复杂。在这里,我们提出了一种新的方法,利用这种模式的预测功能残基。该方法使用了一个简单但强大的整个蛋白质的表示,以及序列残基作为载体,在一个广义的“序列空间”的这些载体投影到一个较低的维度空间揭示了特定的亚家族,有预测直接参与蛋白质功能的残基组。基于该方法,我们提出了可测试的预测组的功能残基在SH2结构域和细胞周期蛋白的保守框。
The biological activity of a protein typically depends on the presence of a small number of functional residues. identifying these residues from the amino acid sequences alone would be useful. Classically, strictly conserved residues are predicted to be functional but often conservation patterns are more complicated. Here, we present a novel method that exploits such patterns for the prediction of functional residues. The method uses a simple but powerful representation of entire proteins, as well as sequence residues as vectors in a generalised 'sequence space' projection of these vectors onto a lower-dimensional space reveals groups of residues specific for particular subfamilies that ave predicted to be directly involved in protein function. Based on the method we present testable predictions for sets of functional residues in SH2 domains and in the conserved box of cyclins.