Protein-protein docking predictions for the CAPRI experiment

TitleProtein-protein docking predictions for the CAPRI experiment
Publication TypeJournal Article
Year of Publication2003
AuthorsGray, J. J., Moughon S. E., Kortemme T., Schueler-Furman O., Misura K. M. S., Morozov A. V., & Baker D.
JournalProteins
Volume52
Issue1
Pagination118-22
Date Published2003 Jul 1
ISSN1097-0134
KeywordsAlgorithms, alpha-Amylases, Amino Acid Sequence, Antibodies, Antigens, Viral, Bacterial Proteins, Binding Sites, Capsid Proteins, Exotoxins, Hemagglutinin Glycoproteins, Influenza Virus, Macromolecular Substances, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Monte Carlo Method, Phosphoenolpyruvate Sugar Phosphotransferase System, Primary Publication, Protein Interaction Mapping, Protein-Serine-Threonine Kinases, Proteins, Receptors, Antigen, T-Cell, alpha-beta, Sequence Alignment
Abstract

We predicted structures for all seven targets in the CAPRI experiment using a new method in development at the time of the challenge. The technique includes a low-resolution rigid body Monte Carlo search followed by high-resolution refinement with side-chain conformational changes and rigid body minimization. Decoys (approximately 10(6) per target) were discriminated using a scoring function including van der Waals and solvation interactions, hydrogen bonding, residue-residue pair statistics, and rotamer probabilities. Decoys were ranked, clustered, manually inspected, and selected. The top ranked model for target 6 predicted the experimental structure to 1.5 A RMSD and included 48 of 65 correct residue-residue contacts. Target 7 was predicted at 5.3 A RMSD with 22 of 37 correct residue-residue contacts using a homology model from a known complex structure. Using a preliminary version of the protocol in round 1, target 1 was predicted within 8.8 A although few contacts were correct. For targets 2 and 3, the interface locations and a small fraction of the contacts were correctly identified.

Alternate JournalProteins
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