MDockPeP: An ab-initio protein-peptide docking server

J Comput Chem. 2018 Oct 30;39(28):2409-2413. doi: 10.1002/jcc.25555. Epub 2018 Oct 23.

Abstract

Protein-peptide interactions play a crucial role in a variety of cellular processes. The protein-peptide complex structure is a key to understand the mechanisms underlying protein-peptide interactions and is critical for peptide therapeutic development. We present a user-friendly protein-peptide docking server, MDockPeP. Starting from a peptide sequence and a protein receptor structure, the MDockPeP Server globally docks the all-atom, flexible peptide to the protein receptor. The produced modes are then evaluated with a statistical potential-based scoring function, ITScorePeP. This method was systematically validated using the peptiDB benchmarking database. At least one near-native peptide binding mode was ranked among top 10 (or top 500) in 59% (85%) of the bound cases, and in 40.6% (71.9%) of the challenging unbound cases. The server can be used for both protein-peptide complex structure prediction and initial-stage sampling of the protein-peptide binding modes for other docking or simulation methods. MDockPeP Server is freely available at http://zougrouptoolkit.missouri.edu/mdockpep. © 2018 Wiley Periodicals, Inc.

Keywords: complex structure prediction; molecular docking; molecular modeling; protein-peptide interactions; web server.

Publication types

  • News
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Computers*
  • Databases, Protein
  • Internet*
  • Molecular Docking Simulation*
  • Peptides / chemistry*
  • Protein Binding
  • Protein Conformation
  • Proteins / chemistry*

Substances

  • Peptides
  • Proteins