Comparative Assessment of Data Sets of Protein Interaction Hot Spots Used in the Computational Method
详细信息    查看全文
  • 作者:Yunqiang Di (21) (22)
    Changchang Wang (21) (23)
    Huan Wu (21) (22)
    Xinxin Yu (21) (24)
    Junfeng Xia (21)
  • 关键词:proteins ; protein interaction ; hot spots ; computational method ; training data
  • 刊名:Lecture Notes in Computer Science
  • 出版年:2014
  • 出版时间:2014
  • 年:2014
  • 卷:8590
  • 期:1
  • 页码:478-486
  • 全文大小:386 KB
  • 参考文献:1. Kortemme, T., Baker, D.: A Simple Physical Model for Binding Energy Hot Spots In Protein–Protein Complexes. Proceedings of the National Academy of Sciences?99(22), 14116-4121 (2002) CrossRef
    2. Walter, P., et al.: Predicting Where Small Molecules Bind at Protein-Protein Interfaces. Plos One?8(3), E58583 (2013)
    3. Liu, Q., et al.: Structural Analysis of the Hot Spots in the Binding Between H1N1 HA and The 2D1 Antibody: Do Mutations of H1N1 From 1918 to 2009 Affect Much on This Binding? Bioinformatics?27(18), 2529-536 (2011)
    4. Liu, Z.-P., et al.: Bridging Protein Local Structures and Protein Functions. Amino Acids?35(3), 627-50 (2008) CrossRef
    5. Cunningham, B.C., Wells, J.A.: High-Resolution Epitope Mapping of Hgh-Receptor Interactions by Alanine-Scanning Mutagenesis. Science?244(4908), 1081-085 (1989) CrossRef
    6. Thorn, K.S., Bogan, A.A.: Asedb: a Database of Alanine Mutations and their Effects on the Free Energy of Binding in Protein Interactions. Bioinformatics?17(3), 284-85 (2001) CrossRef
    7. Fischer, T., et al.: The Binding Interface Database (BID): a Compilation of Amino Acid Hot Spots in Protein Interfaces. Bioinformatics?19(11), 1453-454 (2003) CrossRef
    8. Tuncbag, N., Keskin, O., Gursoy, A.: Hotpoint: Hot Spot Prediction Server for Protein Interfaces. Nucleic Acids Research?38(suppl. 2), W402–W406 (2010)
    9. Darnell, S.J., Legault, L., Mitchell, J.C.: KFC Server: Interactive Forecasting of Protein Interaction Hot Spots. Nucleic Acids Research 36(suppl. 2), W265–W269 (2008)
    10. Cho, K.-I., Kim, D., Lee, D.: A Feature-Based Approach to Modeling Protein–Protein Interaction Hot Spots. Nucleic Acids Research?37(8), 2672-687 (2009) CrossRef
    11. Xia, J.-F., et al.: APIS: Accurate Prediction of Hot Spots in Protein Interfaces by Combining Protrusion Index with Solvent Accessibility. BMC Bioinformatics?11(1), 174 (2010) CrossRef
    12. Ye, L., et al.: Prediction of Hot Spots Residues in Protein–Protein Interface Using Network Feature and Microenvironment Feature. Chemometrics and Intelligent Laboratory Systems?131, 16-1 (2014) CrossRef
    13. Cheng, J., et al.: Training Set Selection for The Prediction of Essential Genes. Plos One?9(1), E86805 (2014)
    14. Zhu, X., Mitchell, J.C.: KFC2: A Knowledge‐Based Hot Spot Prediction Method Based on Interface Solvation, Atomic Density, and Plasticity Features. Proteins: Structure, Function, and Bioinformatics?79(9), 2671-683 (2011) CrossRef
    15. Wang, L., et al.: Prediction of Hot Spots in Protein Interfaces Using a Random Forest Model With Hybrid Features. Protein Engineering Design and Selection?25(3), 119-26 (2012) CrossRef
    16. Wang, L., et al.: Prediction of Hot Spots in Protein Interfaces Using Extreme Learning Machines with the Information of Spatial Neighbour Residues (2014)
    17. Darnell, S.J., Page, D., Mitchell, J.C.: An Automated Decision‐Tree Approach to Predicting Protein Interaction Hot Spots. Proteins: Structure, Function, and Bioinformatics?68(4), 813-23 (2007) CrossRef
    18. Nguyen, Q., Fablet, R., Pastor, D.: Protein Interaction Hotspot Identification Using Sequence-Based Frequency-Derived Features. IEEE Transactions on Biomedical Engineering?60(11), 2993-002 (2013) CrossRef
    19. Liu, Q., et al.: Integrating Water Exclusion Theory Into ? Contacts to Predict Binding Free Energy Changes and Binding Hot Spots. BMC Bioinformatics?15(1), 57 (2014) CrossRef
    20. Xu, B., et al.: A Semi-Supervised Boosting SVM for Predicting Hot Spots at Protein-Protein Interfaces. BMC Systems Biology?6(suppl. 2), S6 (2012)
    21. Tuncbag, N., Gursoy, A., Keskin, O.: Identification of Computational Hot Spots in Protein Interfaces: Combining Solvent Accessibility and Inter-Residue Potentials Improves the Accuracy. Bioinformatics?25(12), 1513-520 (2009) CrossRef
    22. Oliveros, J.C.: VENNY. An Interactive Tool for Comparing Lists with Venn Diagrams (2007)
    23. Mihel, J., et al.: PSAIA–Protein Structure and Interaction Analyzer. BMC Structural Biology?8(1), 21 (2008) CrossRef
    24. Hubbard, S., Thornton, J.: Department of Biochemistry and Molecular Biology, University College London (1993)
  • 作者单位:Yunqiang Di (21) (22)
    Changchang Wang (21) (23)
    Huan Wu (21) (22)
    Xinxin Yu (21) (24)
    Junfeng Xia (21)

    21. Institute of Health Sciences, Anhui University, Hefei, Anhui, 230601, China
    22. College of Electrical Engineering and Automation, Anhui University, Hefei, Anhui, 230601, China
    23. School of Computer Science and Technology, Anhui University, Hefei, Anhui, 230601, China
    24. School of Life Sciences, Anhui University, Hefei, Anhui, 230601, China
  • ISSN:1611-3349
文摘
It seems that every biological process involves multiple protein-protein interactions. Small subsets of residues, which are called “hot spots- contribute to most of the protein-protein binding free energy. Considering its important role in the modulation of protein-protein complexes, a large number of computational methods have been proposed in the prediction of hot spots. In this work, we first collect lots of articles from 2007 to 2014 and select nine typical data sets. Then we compare the nine data sets in different aspects. We find that the maximum number of interface residues used in the previous work is 318, which can be selected as the fittest training data set used in predicting hot spots. At last, we compare and assess the features used in different works. Our result suggests that accessibility and residue conservation are critical in predicting hot spots.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700