ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

DoSA: Database of Structural Alignments

Mahajan, Swapnil and Agarwal, Garima and Iftekhar, Mohammed and Offmann, Bernard and de Brevern, Alexandre G and Srinivasan, Narayanaswamy (2013) DoSA: Database of Structural Alignments. In: DATABASE-THE JOURNAL OF BIOLOGICAL DATABASES AND CURATION, 2013 .

[img]
Preview
PDF
Database-2013-Mahajan-database_bat048.pdf - Published Version

Download (412kB) | Preview
[img] Microsoft Word
DoSA_Supplementary_data_1.doc - Published Supplemental Material

Download (464kB)
Official URL: http://dx.doi.org/10.1093/database/bat048

Abstract

Protein structure alignment is a crucial step in protein structure-function analysis. Despite the advances in protein structure alignment algorithms, some of the local conformationally similar regions are mislabeled as structurally variable regions (SVRs). These regions are not well superimposed because of differences in their spatial orientations. The Database of Structural Alignments (DoSA) addresses this gap in identification of local structural similarities obscured in global protein structural alignments by realigning SVRs using an algorithm based on protein blocks. A set of protein blocks is a structural alphabet that abstracts protein structures into 16 unique local structural motifs. DoSA provides unique information about 159 780 conformationally similar and 56 140 conformationally dissimilar SVRs in 74 705 pairwise structural alignments of homologous proteins. The information provided on conformationally similar and dissimilar SVRs can be helpful to model loop regions. It is also conceivable that conformationally similar SVRs with conserved residues could potentially contribute toward functional integrity of homologues, and hence identifying such SVRs could be helpful in understanding the structural basis of protein function.

Item Type: Journal Article
Publication: DATABASE-THE JOURNAL OF BIOLOGICAL DATABASES AND CURATION
Publisher: OXFORD UNIV PRESS
Additional Information: Copyright of this article belongs to OXFORD UNIV PRESS
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 04 Sep 2013 05:24
Last Modified: 04 Sep 2013 05:25
URI: http://eprints.iisc.ac.in/id/eprint/47039

Actions (login required)

View Item View Item