Assessment of template based protein structure predictions in CASP9
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID
856156
Author(s)
Mariani, Valerio; Kiefer, Florian; Schmidt, Tobias; Haas, Juergen; Schwede, Torsten
Author(s) at UniBasel
Schwede, Torsten Haas, Jürgen
Year
2011
Title
Assessment of template based protein structure predictions in CASP9
Journal
Proteins
Volume
79 Suppl 10
Number
S10
Pages / Article-Number
37-58
Keywords
protein structure, evaluation, structure prediction, CASP
Abstract
In the Ninth Edition of the Critical Assessment of Techniques for Protein Structure Prediction (CASP9), 61,665 models submitted by 176 groups were assessed for their accuracy in the template based modeling category. The models were evaluated numerically in comparison to their experimental control structures using two global measures (GDT and GDC), and a novel local score evaluating the correct modeling of local interactions (lDDT). Overall, the state of the art of template based modeling in CASP9 is high, with many groups performing well. Among the methods registered as prediction "servers", six independent groups are performing on average better than the rest. The submissions by "human" groups are dominated by meta-predictors, with one group performing noticeably better than the others. Most of the participating groups failed to assign realistic confidence estimates to their predictions, and only a very small fraction of the assessed methods have provided highly accurate models and realistic error estimates at the same time. Also, the accuracy of predictions for homo-oligomeric assemblies was overall poor, and only one group performed better than a naïve control predictor. Here, we present the results of our assessment of the CASP9 predictions in the category of template based modeling, documenting the state of the art and highlighting areas for future developments. Proteins 2011; © 2011 Wiley-Liss, Inc.
Publisher
Wiley-Liss
ISSN/ISBN
0887-3585
URL
http://onlinelibrary.wiley.com/doi/10.1002/prot.23177/full
edoc-URL
http://edoc.unibas.ch/dok/A5848281
Full Text on edoc
No
Digital Object Identifier DOI
10.1002/prot.23177
PubMed ID
http://www.ncbi.nlm.nih.gov/pubmed/22002823
ISI-Number
WOS:000297972300004
Document type (ISI)
Journal Article
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