Search tips
Search criteria 


Logo of bioinformLink to Publisher's site
Bioinformation. 2009; 3(6): 263–267.
Published online Jan 12, 2009.
PMCID: PMC2646861
New tips for structure prediction by comparative modeling
Anwar Rayan*
QRC-Qasemi Research Center,Al-Qasemi Academic College, P.O.B. 124, Baka El-Garbiah 30100, Israel
*Anwar Rayan: a_rayan/at/
Received December 13, 2008; Accepted December 29, 2008.
Comparative modelling is utilized to predict the 3-dimensional conformation of a given protein (target) based on its sequence alignment to experimentally determined protein structure (template). The use of such technique is already rewarding and increasingly widespread in biological research and drug development. The accuracy of the predictions as commonly accepted depends on the score of sequence identity of the target protein to the template. To assess the relationship between sequence identity and model quality, we carried out an analysis of a set of 4753 sequence and structure alignments. Throughout this research, the model accuracy was measured by root mean square deviations of Cα atoms of the target-template structures. Surprisingly, the results show that sequence identity of the target protein to the template is not a good descriptor to predict the accuracy of the 3-D structure model. However, in a large number of cases, comparative modelling with lower sequence identity of target to template proteins led to more accurate 3-D structure model. As a consequence of this study, we suggest new tips for improving the quality of omparative models, particularly for models whose target-template sequence identity is below 50%.
Keywords: comparative modelling, homology modelling, model refinement
Articles from Bioinformation are provided here courtesy of
Biomedical Informatics Publishing Group