Comparative analyses of quaternary arrangements in homo-oligomeric proteins in superfamilies: Functional implications

Sudha, Govindarajan and Srinivasan, Narayanaswamy (2016) Comparative analyses of quaternary arrangements in homo-oligomeric proteins in superfamilies: Functional implications. In: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 84 (9). pp. 1190-1202.

PDF Pro_84-9_1190_2016.pdf - Published Version Restricted to Registered users only Download (623kB) | Request a copy

Abstract

A comprehensive analysis of the quaternary features of distantly related homo-oligomeric proteins is the focus of the current study. This study has been performed at the levels of quaternary state, symmetry, and quaternary structure. Quaternary state and quaternary structure refers to the number of subunits and spatial arrangements of subunits, respectively. Using a large dataset of available 3D structures of biologically relevant assemblies, we show that only 53% of the distantly related homo-oligomeric proteins have the same quaternary state. Considering these homologous homo-oligomers with the same quaternary state, conservation of quaternary structures is observed only in 38% of the pairs. In 36% of the pairs of distantly related homo-oligomers with different quaternary states the larger assembly in a pair shows high structural similarity with the entire quaternary structure of the related protein with lower quaternary state and it is referred as Russian doll effect. The differences in quaternary state and structure have been suggested to contribute to the functional diversity. Detailed investigations show that even though the gross functions of many distantly related homo-oligomers are the same, finer level differences in molecular functions are manifested by differences in quaternary states and structures. Comparison of structures of biological assemblies in distantly and closely related homo-oligomeric proteins throughout the study differentiates the effects of sequence divergence on the quaternary structures and function. Knowledge inferred from this study can provide insights for improved protein structure classification and function prediction of homo-oligomers. Proteins 2016; 84:1190-1202. (c) 2016 Wiley Periodicals, Inc.

Item Type:	Journal Article
Publication:	PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Additional Information:	Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	22 Oct 2016 09:20
Last Modified:	22 Oct 2016 09:20
URI:	http://eprints.iisc.ac.in/id/eprint/55012

Actions (login required)

View Item