Title

Fold combinations in multi-domain proteins

Authors

Nagarajan Naveenkumar^1,2,3, Gayatri Kumar³, Ramanathan Sowdhamini¹, Narayanaswamy Srinivasan^*,3 & Sneha Vishwanath³

Affiliation

¹National Center for Biological Science, GKVK Campus, Bengaluru, Karnataka, India – 560065; ²Bharathidasan University, Tiruchirappalli, Tamil Nadu, 620024, India;

³Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka, India – 560012

Email

Narayanaswamy Srinivasan - E-mail: ns@iisc.ac.in; *Corresponding author

Article Type

Research Article

Date

Received May 5, 2019; Accepted May 7, 2019; Published May 15, 2019

Domain-domain interactions in multi-domain proteins play an important role in the combined function of individual domains for the overall biological activity of the protein. The functions of the tethered domains are often coupled and hence, limited numbers of domain architectures with defined folds are known in nature. Therefore, it is of interest to document the available fold-fold combinations and their preference in multi-domain proteins. Hence, we analyzed all multi-domain proteins with known structures in the protein databank and observed that only about 860 fold-fold combinations are present among them. Analyses of multi-domain proteins represented in sequence
database result in recognition of 29,860 fold-fold combinations and it accounts for only 2.8% of the theoretically possible 1,036,080 (1439C2) fold-fold combinations. The observed preference for fold-fold combinations in multi-domain proteins is interesting in the context of multiple functions through structural adaptation by gene fusion.

Keywords

domain architecture; domain folds; multi-domain proteins; protein evolution; protein structure

Citation

Naveenkumar et al. Bioinformation 15(5): 342-350 (2019)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.