Joseph, Agnel Praveen and Valadie, Helene and Srinivasan, Narayanaswamy and de Brevern, Alexandre G. (2012) Local Structural Differences in Homologous Proteins: Specificities in Different SCOP Classes. In: PLOS ONE, 7 (6).
|
PDF
Plose_one_7-6_e38805_2012.pdf - Published Version Download (5MB) | Preview |
Abstract
The constant increase in the number of solved protein structures is of great help in understanding the basic principles behind protein folding and evolution. 3-D structural knowledge is valuable in designing and developing methods for comparison, modelling and prediction of protein structures. These approaches for structure analysis can be directly implicated in studying protein function and for drug design. The backbone of a protein structure favours certain local conformations which include alpha-helices, beta-strands and turns. Libraries of limited number of local conformations (Structural Alphabets) were developed in the past to obtain a useful categorization of backbone conformation. Protein Block (PB) is one such Structural Alphabet that gave a reasonable structure approximation of 0.42 angstrom. In this study, we use PB description of local structures to analyse conformations that are preferred sites for structural variations and insertions, among group of related folds. This knowledge can be utilized in improving tools for structure comparison that work by analysing local structure similarities. Conformational differences between homologous proteins are known to occur often in the regions comprising turns and loops. Interestingly, these differences are found to have specific preferences depending upon the structural classes of proteins. Such class-specific preferences are mainly seen in the all-beta class with changes involving short helical conformations and hairpin turns. A test carried out on a benchmark dataset also indicates that the use of knowledge on the class specific variations can improve the performance of a PB based structure comparison approach. The preference for the indel sites also seem to be confined to a few backbone conformations involving beta-turns and helix C-caps. These are mainly associated with short loops joining the regular secondary structures that mediate a reversal in the chain direction. Rare beta-turns of type I' and II' are also identified as preferred sites for insertions.
| Item Type: | Journal Article |
|---|---|
| Publication: | PLOS ONE |
| Publisher: | PUBLIC LIBRARY SCIENCE |
| Additional Information: | Copy right for this article belongs to Joseph et al. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 09 Aug 2012 11:30 |
| Last Modified: | 09 Aug 2012 11:30 |
| URI: | http://eprints.iisc.ac.in/id/eprint/44925 |
Actions (login required)
 |
View Item |
