Structural Bioinformatics Group, Division of Molecular Biosciences, Imperial College London, South Kensington, London, UK.
Curr Opin Struct Biol. 2011 Jun;21(3):382-90. doi: 10.1016/j.sbi.2011.03.013. Epub 2011 Apr 14.
Macromolecular interactions are central to most cellular processes. Experimental methods generate diverse data on these interactions ranging from high throughput protein-protein interactions (PPIs) to the crystallised structures of complexes. Despite this, only a fraction of interactions have been identified and therefore predictive methods are essential to fill in the numerous gaps. Many predictive methods use information from related proteins. Accordingly, we review the conservation of interface and ligand binding sites within protein families and their association with conserved residues and Specificity Determining Positions. We then review recent developments in predictive methods for the identification of PPIs, protein interface sites and small molecule ligand binding sites. The challenges that are still faced by the community in these areas are discussed.
大分子相互作用是大多数细胞过程的核心。实验方法生成了关于这些相互作用的各种数据，从高通量的蛋白质-蛋白质相互作用 (PPIs) 到复合物的结晶结构。尽管如此，只有一部分相互作用已经被确定，因此预测方法对于填补众多空白至关重要。许多预测方法都使用来自相关蛋白质的信息。因此，我们回顾了蛋白质家族中界面和配体结合位点的保守性及其与保守残基和特异性决定位置的关系。然后，我们回顾了最近用于识别 PPIs、蛋白质界面位点和小分子配体结合位点的预测方法的发展。讨论了该领域仍然面临的挑战。
