Assessment of template based protein structure predictions in CASP9

被引:128
作者
Mariani, Valerio [2 ]
Kiefer, Florian [2 ]
Schmidt, Tobias [2 ]
Haas, Juergen [2 ]
Schwede, Torsten [1 ,2 ]
机构
[1] Univ Basel, Biozentrum, SIB, Swiss Inst Bioinformat, CH-4056 Basel, Switzerland
[2] SIB Swiss Inst Bioinformat, Basel, Switzerland
关键词
protein structure; evaluation; structure prediction; CASP; DOMAIN DEFINITION; MODELS; CLASSIFICATION; ALIGNMENTS; ACCURACY;
D O I
10.1002/prot.23177
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (IDDT). 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 naive 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; 79(Suppl 10): 37-58. (C) 2011 Wiley-Liss, Inc.
引用
收藏
页码:37 / 58
页数:22
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