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Sequence and Structure-Based Analyses of Human Ankyrin Repeats
Ankyrin is one of the most abundant protein repeat families found across all forms of life. It is found in a variety of multi-domain and single domain proteins in humans with diverse number of repeating units. They are observed to occur in several functionally diverse proteins, such as transcription...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8781854/ https://www.ncbi.nlm.nih.gov/pubmed/35056738 http://dx.doi.org/10.3390/molecules27020423 |
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author | Chakrabarty, Broto Parekh, Nita |
author_facet | Chakrabarty, Broto Parekh, Nita |
author_sort | Chakrabarty, Broto |
collection | PubMed |
description | Ankyrin is one of the most abundant protein repeat families found across all forms of life. It is found in a variety of multi-domain and single domain proteins in humans with diverse number of repeating units. They are observed to occur in several functionally diverse proteins, such as transcriptional initiators, cell cycle regulators, cytoskeletal organizers, ion transporters, signal transducers, developmental regulators, and toxins, and, consequently, defects in ankyrin repeat proteins have been associated with a number of human diseases. In this study, we have classified the human ankyrin proteins into clusters based on the sequence similarity in their ankyrin repeat domains. We analyzed the amino acid compositional bias and consensus ankyrin motif sequence of the clusters to understand the diversity of the human ankyrin proteins. We carried out network-based structural analysis of human ankyrin proteins across different clusters and showed the association of conserved residues with topologically important residues identified by network centrality measures. The analysis of conserved and structurally important residues helps in understanding their role in structural stability and function of these proteins. In this paper, we also discuss the significance of these conserved residues in disease association across the human ankyrin protein clusters. |
format | Online Article Text |
id | pubmed-8781854 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87818542022-01-22 Sequence and Structure-Based Analyses of Human Ankyrin Repeats Chakrabarty, Broto Parekh, Nita Molecules Article Ankyrin is one of the most abundant protein repeat families found across all forms of life. It is found in a variety of multi-domain and single domain proteins in humans with diverse number of repeating units. They are observed to occur in several functionally diverse proteins, such as transcriptional initiators, cell cycle regulators, cytoskeletal organizers, ion transporters, signal transducers, developmental regulators, and toxins, and, consequently, defects in ankyrin repeat proteins have been associated with a number of human diseases. In this study, we have classified the human ankyrin proteins into clusters based on the sequence similarity in their ankyrin repeat domains. We analyzed the amino acid compositional bias and consensus ankyrin motif sequence of the clusters to understand the diversity of the human ankyrin proteins. We carried out network-based structural analysis of human ankyrin proteins across different clusters and showed the association of conserved residues with topologically important residues identified by network centrality measures. The analysis of conserved and structurally important residues helps in understanding their role in structural stability and function of these proteins. In this paper, we also discuss the significance of these conserved residues in disease association across the human ankyrin protein clusters. MDPI 2022-01-10 /pmc/articles/PMC8781854/ /pubmed/35056738 http://dx.doi.org/10.3390/molecules27020423 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Chakrabarty, Broto Parekh, Nita Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title | Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title_full | Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title_fullStr | Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title_full_unstemmed | Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title_short | Sequence and Structure-Based Analyses of Human Ankyrin Repeats |
title_sort | sequence and structure-based analyses of human ankyrin repeats |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8781854/ https://www.ncbi.nlm.nih.gov/pubmed/35056738 http://dx.doi.org/10.3390/molecules27020423 |
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