- Global distance test
The global distance test or GDT (also written as GDT_TS to represent "total score") is a measure of similarity between two
protein structure s with identicalamino acid sequence s but differenttertiary structure s. It is most commonly used to compare the results ofprotein structure prediction to the experimentally determined structure as measured byX-ray crystallography orprotein NMR . The metric is intended as a more accurate measurement than the more common RMSD metric, which is sensitive tooutlier regions created by poor modeling of individual loop regions in a structure that is otherwise reasonably accurate. GDT_TS measurements are used as major assessment criteria in the production of results from the Critical Assessment of Structure Prediction (CASP), a large-scale experiment in the structure prediction community dedicated to assessing current modeling techniques and identifying their primary deficiencies.The GDT score is calculated as the largest set of
amino acid residues'alpha carbon atoms in the model structure falling within a defined distance cutoff of their position in the experimental structure. It is typical to calculate the GDT score under several cutoff distances, and scores generally increase with increasing cutoff. A plateau in this increase may indicate an extreme divergence between the experimental and predicted structures, such that no additional atoms are included in any cutoff of a reasonable distance.The high accuracy version of the GDT measure is called GDT-HA. It uses smaller cut off distances (half the size of GDT_TS) and thus is more rigorous. [Read 2007.]
External links
* [http://www2.predictioncenter.org/casp/casp6/public/cgi-bin/results.cgi CASP6 results] plotted by GDT score for each target structure included in the experiment
Notes
References
* Zemla A, Venclovas C, Moult J, Fidelis K. (2001). Processing and evaluation of predictions in CASP4. "PROTEINS Structure, Function, and Genetics", 45(S5):13-21.
* Zemla A. (2003). LGA - A Method for Finding 3-D Similarities in Protein Structures. "Nucleic Acids Research", 31(13):3370-3374.
*cite journal
first=Randy J.
last=Read
coauthors=Chavali, Gayatri
title=Assessment of CASP7 predictions in the high accuracy template-based modeling category
journal=Proteins: Structure, Function, and Bioinformatics
volume=69
issue=S8
pages=27-37
id= doi|10.1002/prot.21662
date=2007
accessdate=2008-04-17
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