Figures
Matching drug binding pockets in protein models using sequence order-independent structure alignments.
Drugs are typically developed to modulate the function of specific proteins, which are directly associated with particular disease states. Nonetheless, protein-drug interactions are rather promiscuous and the majority of pharmaceuticals exhibit activity against multiple, often unrelated targets; for instance, ATP-dependent DNA ligase and histamine N-methyltransferase shown here bind the same compound. To detect those binding sites having the capability to bind similar molecules, Michal Brylinski developed eMatchSite, which constructs local sequence order-independent alignments using computer-generated protein models. This approach opens up the possibility to investigate drug-protein interactions for complete proteomes with prospective systems-level applications in polypharmacology and rational drug repositioning.
Image Credit: Michal Brylinski
Citation: (2014) PLoS Computational Biology Issue Image | Vol. 10(9) September 2014. PLoS Comput Biol 10(9): ev10.i09. https://doi.org/10.1371/image.pcbi.v10.i09
Published: September 25, 2014
Copyright: © 2014 Michal Brylinski. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Drugs are typically developed to modulate the function of specific proteins, which are directly associated with particular disease states. Nonetheless, protein-drug interactions are rather promiscuous and the majority of pharmaceuticals exhibit activity against multiple, often unrelated targets; for instance, ATP-dependent DNA ligase and histamine N-methyltransferase shown here bind the same compound. To detect those binding sites having the capability to bind similar molecules, Michal Brylinski developed eMatchSite, which constructs local sequence order-independent alignments using computer-generated protein models. This approach opens up the possibility to investigate drug-protein interactions for complete proteomes with prospective systems-level applications in polypharmacology and rational drug repositioning.
Image Credit: Michal Brylinski