What is it about?
This research investigation is concerning a protein-peptide interaction observed in the model plant Arabidopsis thaliana. The peptide, AtPep1, is implied in innate immunity (defense peptide). Its interaction with cell-surface receptor PEPR1 has been probed using an array of computational techniques (sequence analysis, structure and order prediction, homology modelling, molecular dynamics and docking) in this research work.
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Why is it important?
At the time when this investigation was taken up for computational analysis, there was no structure of either the protein or peptide or the complex. Hence, considerable time was spent in understanding the peptide conformation. The receptor could be modeled accurately as a highly similar protein crystal structure from A. thaliana itself was available. Hence, this study provides a working methodology for investigating protein-peptide interactions.
Perspectives
I designed and executed the entire work in this investigation as a forerunner to my studies on protein-peptide interactions. This study did shed light on a promiscuous protein-peptide interaction at a molecular level. Upon the availability of a crystal structure of the complex, after the publication of our research, it became extremely clear that the binding region (interface) and the peptide conformation at the interaction site predictions could be well improved to mimic the actual biological interaction.
Dr. Raghavender S Upadhyayula
Centre for DNA Fingerprinting & Diagnostics
Read the Original
This page is a summary of: Mechanistic Basis Of Peptide-Protein Interaction In AtPep1-PEPR1 Complex In Arabidopsis thaliana, Protein and Peptide Letters, June 2015, Bentham Science Publishers,
DOI: 10.2174/0929866522666150506154201.
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