A state of the art protein-protein docking program
The top 1000 (near-native) structures generated by ZDOCK for the complex 1ACB contains 89 hits, whereas the number of hits in 1000 structures generated by PIPER is 632. - Kozakov, D., Brenke, R., Comeau, S. R. and Vajda, S., ''PIPER: an FFT-based protein docking program with pairwise potentials,'' Proteins, 2006, 65(2), 392-406
PIPER: A state of the art protein-protein docking program
PIPER is a state-of-the-art protein-protein docking program based on a multi-staged approach and advanced numerical methods that reliably generates accurate structures of protein-protein complexes. Based on well-validated docking code from the Vajda lab at Boston University, PIPER has a proven track record as an outstanding predictor of protein-protein complexes as judged by previous CAPRI (Critical Assessment of Prediction of Interactions) blind experiments.
The Advantages of Protein-Protein Docking
Protein-protein interactions govern various aspects of structural and functional cellular mechanisms, and their elucidation is crucial for a better understanding of processes such as metabolic control, signal transduction, and gene regulation. While genome-wide proteomics studies provide an increasing list of interacting proteins, only a small fraction of the potential complexes are amenable to direct experimental analysis. Thus, it is important to utilize protein-protein docking methods that can explain the details of specific interactions at the atomic level. Furthermore, the precise understanding of protein-protein interactions for disease-implicated targets is ever more critical for the rational design of biologic-based therapies.
For more information please visit the PIPER website.
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