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Fold combinations in multi-domain proteins

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...

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Autores principales: Naveenkumar, Nagarajan, Kumar, Gayatri, Sowdhamini, Ramanathan, Srinivasan, Narayanaswamy, Vishwanath, Sneha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589474/
https://www.ncbi.nlm.nih.gov/pubmed/31249437
http://dx.doi.org/10.6026/97320630015342
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author Naveenkumar, Nagarajan
Kumar, Gayatri
Sowdhamini, Ramanathan
Srinivasan, Narayanaswamy
Vishwanath, Sneha
author_facet Naveenkumar, Nagarajan
Kumar, Gayatri
Sowdhamini, Ramanathan
Srinivasan, Narayanaswamy
Vishwanath, Sneha
author_sort Naveenkumar, Nagarajan
collection PubMed
description 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.
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spelling pubmed-65894742019-06-27 Fold combinations in multi-domain proteins Naveenkumar, Nagarajan Kumar, Gayatri Sowdhamini, Ramanathan Srinivasan, Narayanaswamy Vishwanath, Sneha Bioinformation Research Article 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. Biomedical Informatics 2019-05-15 /pmc/articles/PMC6589474/ /pubmed/31249437 http://dx.doi.org/10.6026/97320630015342 Text en © 2019 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ 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.
spellingShingle Research Article
Naveenkumar, Nagarajan
Kumar, Gayatri
Sowdhamini, Ramanathan
Srinivasan, Narayanaswamy
Vishwanath, Sneha
Fold combinations in multi-domain proteins
title Fold combinations in multi-domain proteins
title_full Fold combinations in multi-domain proteins
title_fullStr Fold combinations in multi-domain proteins
title_full_unstemmed Fold combinations in multi-domain proteins
title_short Fold combinations in multi-domain proteins
title_sort fold combinations in multi-domain proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589474/
https://www.ncbi.nlm.nih.gov/pubmed/31249437
http://dx.doi.org/10.6026/97320630015342
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