Systematic assessment of accuracy of comparative model of proteins belonging to different structural fold classes.

ABSTRACT: In the absence of experimental structures, comparative modeling continues to be the chosen method for retrieving structural information on target proteins. However, models lack the accuracy of experimental structures. Alignment error and structural divergence (between target and template) influence model accuracy the most. Here, we examine the potential additional impact of backbone geometry, as our previous studies have suggested that the structural class (all-α, αβ, all-β) of a protein may influence the accuracy of its model. In the twilight zone (sequence identity ≤ 30%) and at a similar level of target-template divergence, the accuracy of protein models does indeed follow the trend all-α > αβ > all-β. This is mainly because the alignment accuracy follows the same trend (all-α > αβ > al

SUBMITTER: Chakravarty S 

PROVIDER: S-EPMC3204187 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature