Prediction of Dipeptidyl Peptidase (DP) 8 Structure by Homology Modelling

  • Melissa R. Pitman
  • R. Ian Menz
  • Catherine A. Abbott
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (volume 575)

5. Conclusions

The DP8 model produced was very similar to the DPIV structure in the α/β hydrolase domain. Analysis of the active site of the DP8 model revealed significant structural conservation in the catalytic triad between DPIV, PEP and ACPH. Further analysis is required to determine whether any differences in the substrate pockets or substrate access tunnel(s) may contribute to DP8’s ability to act as a dipeptidyl peptidase, endopeptidase and acylaminoacyl peptidase. As the structure of fibroblast activation protein has recently been published, an alternative model may be made using this structure together with DPIV to make a model based on two enzymatically active proteins. Simulated docking of substrates and inhibitors into the model may uncover subtle differences between the structures. This may aid in determining the reason for DP8’s multiple enzyme functionality and aid in the improvement of DPIV inhibitor specificity.


Root Mean Square Deviation Catalytic Triad Template Structure Dipeptidyl Peptidase Fibroblast Activation Protein 
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Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • Melissa R. Pitman
    • 1
  • R. Ian Menz
    • 1
  • Catherine A. Abbott
    • 1
  1. 1.School of Biological SciencesFlinders UniversityAdelaideAustralia

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