Improving CAPRI predictions: optimized desolvation for rigid-body docking

Proteins. 2005 Aug 1;60(2):308-13. doi: 10.1002/prot.20575.

Abstract

The ICM Docking and Interface Side-Chain Optimization (ICM-DISCO) showed promising predictive results during the first CAPRI experiment by successfully finding medium- or high-accuracy models in 3 of the 7 targets. A key factor was the ability to recognize near-native rigid-body geometries in a relatively low number of alternative docking poses, together with the successful refinement of the rigid-body docking interfaces. Since then, we have focused on improving the scoring function to optimally discriminate the near-native rigid-body conformations. For that, we have defined a new desolvation descriptor for rigid-body docking, based on atomic solvation parameters (ASPs) derived from octanol-water transfer experiments. This and other new approaches have been gradually incorporated into our docking procedure during our participation on the second CAPRI experiment. Overall, we produced reasonable models for 8 of the 9 official targets. Especially encouraging were those cases in which a homology model of 1 of the subunits had to be used during the docking simulations. And not less gratifying has been the successful prediction of antibody-antigen targets in a completely automatic, unrestrained fashion. In summary, our success rate (89%) shows a consistent improvement over the previous CAPRI rounds, and suggests that a correct desolvation description is key for improved protein-protein docking predictions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Animals
  • Bacterial Proteins / chemistry
  • Binding Sites
  • Computational Biology / methods*
  • Computer Simulation
  • Crystallography, X-Ray
  • Databases, Protein
  • Dimerization
  • Internet
  • Macromolecular Substances
  • Models, Molecular
  • Models, Statistical
  • Molecular Conformation
  • Protein Binding*
  • Protein Conformation
  • Protein Folding
  • Protein Interaction Mapping / methods*
  • Protein Structure, Tertiary
  • Proteomics / methods*
  • Reproducibility of Results
  • Sequence Alignment
  • Software
  • Static Electricity
  • Structural Homology, Protein

Substances

  • Bacterial Proteins
  • Macromolecular Substances