IMP  2.2.1
The Integrative Modeling Platform
IMP.integrative_docking

Integrative Docking

This is a protocol for pairwise protein docking, in which additional experimental information about the protein-protein complex is incorporated into the docking procedure to greatly improve the accuracy of predictions. This method succeeds in producing a near-native model among the top 10 models in 42–82% of cases, while state-of-the-art docking methods succeed only in 30–40% of cases, depending on the benchmark and accuracy criterion.

The protocol can currently incorporate data from the following sources:

  • a SAXS profile (SAXS)
  • 2D class average images of the complex from negative-stain EM micrographs (EM2D)
  • a 3D density map of the complex (EM3D)
  • residue type content at the protein interface from NMR spectroscopy (NMR-RTC)
  • chemical cross-linking detected by mass spectrometry (CXMS).

Additionally the protocol can calculate SOAP score based on an atomic statistical potential.

  • a SOAP score (SOAP)

The protocol proceeds by first sampling complex models using PatchDock for pairwise protein docking, followed by filtering based on fit to the experimental data, conformational refinement using FiberDock and composite scoring. Third, good-scoring representatives of clusters of models are picked as final models.

Examples:

Info

Author(s): Dina Schneidman

Maintainer: duhovka

License: LGPL This library is free software; you can redistribute it and/or modify it under the terms of the GNU Lesser General Public License as published by the Free Software Foundation; either version 2 of the License, or (at your option) any later version.

Publications:

  • Schneidman-Duhovny D, Hammel M, Sali A. Macromolecular docking restrained by a small angle X-ray scattering profile. J Struct Biol. 2011 Mar;173(3):461-71.
  • Schneidman-Duhovny et al. A method for integrative structure determination of protein-protein complexes. Bioinformatics. 2012;28(24):3282-9.
  • Dong GQ, Fan H, Schneidman-Duhovny D, Webb B, Sali A. Optimized atomic statistical potentials: Assessment of protein interfaces and loops. submitted.