Zhou Huan-Xiang, Qin Sanbo
Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
Bioinformatics. 2007 Sep 1;23(17):2203-9. doi: 10.1093/bioinformatics/btm323. Epub 2007 Jun 22.
Proteins function through interactions with other proteins and biomolecules. Protein-protein interfaces hold key information toward molecular understanding of protein function. In the past few years, there have been intensive efforts in developing methods for predicting protein interface residues. A review that presents the current status of interface prediction and an overview of its applications and project future developments is in order.
Interface prediction methods rely on a wide range of sequence, structural and physical attributes that distinguish interface residues from non-interface surface residues. The input data are manipulated into either a numerical value or a probability representing the potential for a residue to be inside a protein interface. Predictions are now satisfactory for complex-forming proteins that are well represented in the Protein Data Bank, but less so for under-represented ones. Future developments will be directed at tackling problems such as building structural models for multi-component structural complexes.
蛋白质通过与其他蛋白质和生物分子的相互作用发挥功能。蛋白质-蛋白质界面对于从分子层面理解蛋白质功能至关重要。在过去几年中，人们致力于开发预测蛋白质界面残基的方法。因此，有必要对界面预测的现状、其应用进行综述并展望未来发展。
界面预测方法依赖于多种序列、结构和物理属性，这些属性将界面残基与非界面表面残基区分开来。输入数据被处理为数值或概率，以表示残基位于蛋白质界面内的可能性。对于在蛋白质数据库中有良好代表性的形成复合物的蛋白质，目前的预测结果令人满意，但对于代表性不足的蛋白质，预测效果则较差。未来的发展将致力于解决诸如构建多组分结构复合物的结构模型等问题。
