Peptiderive server: derive peptide inhibitors from protein–protein interactions
By Yuval Sedan, Orly Marcu, Sergey Lyskov, O. Schueler‐Furman. 2016
97 citations recorded by the source corpus.
The Rosetta Peptiderive protocol identifies, in a given structure of a protein–protein interaction, the linear polypeptide segment suggested to contribute most to binding energy. Interactions that feature a ‘hot segment’, a linear peptide with significant binding energy compared to that of the complex, may be amenable for inhibition and the peptide sequence and structure derived from the interaction provide a starting point for rational drug design. Here we present a web server for Peptiderive, which is incorporated within the ROSIE web interface for Rosetta protocols. A new feature of the protocol also evaluates whether derived peptides are good candidates for cyclization. Fast computation times and clear visualization allow users to quickly assess the interaction of interest. The Peptiderive server is available for free use at http://rosie.rosettacommons.org/peptiderive.
Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging
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In Molecular Biology
- Jeffrey J. Gray
- Jens Meiler
- Sergey Lyskov
- Rhiju Das
- Rocco Moretti
- David Baker
- Brian D. Weitzner
- Tanja Kortemme
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Web‐accessible molecular modeling with Rosetta: The Rosetta Online Server that Includes Everyone (ROSIE) (2018, background): “56,57 These peptides can then potentially be used as inhibitors of the protein–protein interaction.”