Biological function derived from predicted structures in CASP11.

TitleBiological function derived from predicted structures in CASP11.
Publication TypeJournal Article
Year of Publication2016
AuthorsHuwe PJ, Xu Q, Shapovalov MV, Modi V, Andrake MD, Dunbrack RL
JournalProteins
Volume84 Suppl 1
Pagination370-91
Date Published2016 Sep
ISSN1097-0134
KeywordsAmidohydrolases, Binding Sites, Computational Biology, Cyclic AMP-Dependent Protein Kinases, GPI-Linked Proteins, Hepatocyte Growth Factor, HIV Envelope Protein gp120, Humans, Ligands, Models, Statistical, Molecular Docking Simulation, Mutation, Missense, Phenotype, Protein Binding, Protein Domains, Protein Folding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Proto-Oncogene Proteins, Sequence Homology, Amino Acid, Structure-Activity Relationship, Thermodynamics
Abstract

In CASP11, the organizers sought to bring the biological inferences from predicted structures to the fore. To accomplish this, we assessed the models for their ability to perform quantifiable tasks related to biological function. First, for 10 targets that were probable homodimers, we measured the accuracy of docking the models into homodimers as a function of GDT-TS of the monomers, which produced characteristic L-shaped plots. At low GDT-TS, none of the models could be docked correctly as homodimers. Above GDT-TS of ∼60%, some models formed correct homodimers in one of the largest docked clusters, while many other models at the same values of GDT-TS did not. Docking was more successful when many of the templates shared the same homodimer. Second, we docked a ligand from an experimental structure into each of the models of one of the targets. Docking to the models with two different programs produced poor ligand RMSDs with the experimental structure. Measures that evaluated similarity of contacts were reasonable for some of the models, although there was not a significant correlation with model accuracy. Finally, we assessed whether models would be useful in predicting the phenotypes of missense mutations in three human targets by comparing features calculated from the models with those calculated from the experimental structures. The models were successful in reproducing accessible surface areas but there was little correlation of model accuracy with calculation of FoldX evaluation of the change in free energy between the wild-type and the mutant. Proteins 2016; 84(Suppl 1):370-391. © 2016 Wiley Periodicals, Inc.

DOI10.1002/prot.24997
Alternate JournalProteins
PubMed ID27181425
PubMed Central IDPMC4963311
Grant ListP30 CA006927 / CA / NCI NIH HHS / United States
R01 GM084453 / GM / NIGMS NIH HHS / United States
T32 CA009035 / CA / NCI NIH HHS / United States