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A Comparison of Rosetta Stones in Adapter Protein Families
The inventory of proteins used in different kingdoms appears surprisingly similar in all sequenced eukaryotic genome. Protein domains represent the basic evolutionary units that form proteins. Domain duplication and shuffling by recombination are probably the most important forces driving protein ev...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295043/ https://www.ncbi.nlm.nih.gov/pubmed/28246462 http://dx.doi.org/10.6026/97320630012285 |
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author | Kumar, Hulikal Shivashankara Santosh Kumar, Vadlapudi |
author_facet | Kumar, Hulikal Shivashankara Santosh Kumar, Vadlapudi |
author_sort | Kumar, Hulikal Shivashankara Santosh |
collection | PubMed |
description | The inventory of proteins used in different kingdoms appears surprisingly similar in all sequenced eukaryotic genome. Protein domains represent the basic evolutionary units that form proteins. Domain duplication and shuffling by recombination are probably the most important forces driving protein evolution and hence the complexity of the proteome. While the duplication of whole genes as well as domain encoding exons increases the abundance of domains in the proteome, domain shuffling increases versatility, i.e. the number of distinct contexts in which a domain can occur. In this study we considered five important adapter domain families namely WD40, KELCH, Ankyrin, PDZ and Pleckstrin Homology (PH domain) family for the comparison of Domain versatility, Abundance and domain sharing between them. We used ecological statistics methods such as Jaccard’s Similarity Index (JSI), Detrended Correspondence Analysis, k-Means clustering for the domain distribution data. We found high propensity of domain sharing between PH and PDZ. We found higher abundance of only few selected domains in PH, PDZ, ANK and KELCH families. We also found WD40 family with high versatility and less redundant domain occurrence, with less domain sharing. Hence, the assignments of functions to more orphan WD40 proteins that will help in the identification of suitable drug targets. |
format | Online Article Text |
id | pubmed-5295043 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-52950432017-02-28 A Comparison of Rosetta Stones in Adapter Protein Families Kumar, Hulikal Shivashankara Santosh Kumar, Vadlapudi Bioinformation Hypothesis The inventory of proteins used in different kingdoms appears surprisingly similar in all sequenced eukaryotic genome. Protein domains represent the basic evolutionary units that form proteins. Domain duplication and shuffling by recombination are probably the most important forces driving protein evolution and hence the complexity of the proteome. While the duplication of whole genes as well as domain encoding exons increases the abundance of domains in the proteome, domain shuffling increases versatility, i.e. the number of distinct contexts in which a domain can occur. In this study we considered five important adapter domain families namely WD40, KELCH, Ankyrin, PDZ and Pleckstrin Homology (PH domain) family for the comparison of Domain versatility, Abundance and domain sharing between them. We used ecological statistics methods such as Jaccard’s Similarity Index (JSI), Detrended Correspondence Analysis, k-Means clustering for the domain distribution data. We found high propensity of domain sharing between PH and PDZ. We found higher abundance of only few selected domains in PH, PDZ, ANK and KELCH families. We also found WD40 family with high versatility and less redundant domain occurrence, with less domain sharing. Hence, the assignments of functions to more orphan WD40 proteins that will help in the identification of suitable drug targets. Biomedical Informatics 2016-08-15 /pmc/articles/PMC5295043/ /pubmed/28246462 http://dx.doi.org/10.6026/97320630012285 Text en © 2016 Biomedical Informatics 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 | Hypothesis Kumar, Hulikal Shivashankara Santosh Kumar, Vadlapudi A Comparison of Rosetta Stones in Adapter Protein Families |
title | A Comparison of Rosetta Stones in Adapter Protein Families |
title_full | A Comparison of Rosetta Stones in Adapter Protein Families |
title_fullStr | A Comparison of Rosetta Stones in Adapter Protein Families |
title_full_unstemmed | A Comparison of Rosetta Stones in Adapter Protein Families |
title_short | A Comparison of Rosetta Stones in Adapter Protein Families |
title_sort | comparison of rosetta stones in adapter protein families |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295043/ https://www.ncbi.nlm.nih.gov/pubmed/28246462 http://dx.doi.org/10.6026/97320630012285 |
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