• DocumentCode
    3491210
  • Title

    Protein interaction prediction for mouse pdz domains using dipeptide composition features

  • Author

    Nakariyakul, Songyot ; Liu, Zhi-Ping ; Chen, Luonan

  • Author_Institution
    Key Lab. of Syst. Biol., Chinese Acad. of Sci., Shanghai, China
  • fYear
    2011
  • fDate
    2-4 Sept. 2011
  • Firstpage
    129
  • Lastpage
    132
  • Abstract
    The PDZ domain is one of the largest families of protein domains that are involved in targeting and routing specific proteins in signaling pathways. PDZ domains mediate protein-protein interactions by binding the C-terminal peptides of their target proteins. Using the dipeptide feature encoding, we develop a PDZ domain interaction predictor using a support vector machine that achieves a high accuracy rate of 82.49%. Since most of the dipeptide compositions are redundant and irrelevant, we propose a new hybrid feature selection technique to select only a subset of these compositions that are useful for interaction prediction. Our experimental results show that only approximately 25% of dipeptide features are needed and that our method increases the accuracy by 3%. The selected dipeptide features are analyzed and shown to have important roles on specificity pattern of PDZ domains.
  • Keywords
    biological techniques; biology computing; feature extraction; macromolecules; molecular biophysics; proteins; support vector machines; dipeptide composition; dipeptide feature encoding; hybrid feature selection; mouse PDZ domain; protein binding; protein interaction prediction; protein-protein interaction; signaling pathway; specificity pattern; support vector machine; Accuracy; Amino acids; Encoding; Peptides; Prediction algorithms; Proteins; Support vector machines; Dipeptide compositions; PDZ domain; feature selection; protein interaction;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Systems Biology (ISB), 2011 IEEE International Conference on
  • Conference_Location
    Zhuhai
  • Print_ISBN
    978-1-4577-1661-4
  • Electronic_ISBN
    978-1-4577-1665-2
  • Type

    conf

  • DOI
    10.1109/ISB.2011.6033143
  • Filename
    6033143