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Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins
A fundamental goal in cellular signaling is to understand allosteric communication, the process by which signals originating at one site in a protein propagate reliably to affect distant functional sites. The general principles of protein structure that underlie this process remain unknown. Statisti...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Editorial Department of Journal of Biomedical Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597060/ https://www.ncbi.nlm.nih.gov/pubmed/23554685 http://dx.doi.org/10.1016/S1674-8301(11)60021-3 |
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author | Baths, Veeky Roy, Utpal |
author_facet | Baths, Veeky Roy, Utpal |
author_sort | Baths, Veeky |
collection | PubMed |
description | A fundamental goal in cellular signaling is to understand allosteric communication, the process by which signals originating at one site in a protein propagate reliably to affect distant functional sites. The general principles of protein structure that underlie this process remain unknown. Statistical coupling analysis (SCA) is a statistical technique that uses evolutionary data of a protein family to measure correlation between distant functional sites and suggests allosteric communication. In proteins, very distant and small interactions between collections of amino acids provide the communication which can be important for signaling process. In this paper, we present the SCA of protein alignment of the esterase family (pfam ID: PF00756) containing the sequence of antigen 85C secreted by Mycobacterium tuberculosis to identify a subset of interacting residues. Clustering analysis of the pairwise correlation highlighted seven important residue positions in the esterase family alignments. These residues were then mapped on the crystal structure of antigen 85C (PDB ID: 1DQZ). The mapping revealed correlation between 3 distant residues (Asp38, Leu123 and Met125) and suggests allosteric communication between them. This information can be used for a new drug against this fatal disease. |
format | Online Article Text |
id | pubmed-3597060 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Editorial Department of Journal of Biomedical Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-35970602013-04-02 Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins Baths, Veeky Roy, Utpal J Biomed Res Research Paper A fundamental goal in cellular signaling is to understand allosteric communication, the process by which signals originating at one site in a protein propagate reliably to affect distant functional sites. The general principles of protein structure that underlie this process remain unknown. Statistical coupling analysis (SCA) is a statistical technique that uses evolutionary data of a protein family to measure correlation between distant functional sites and suggests allosteric communication. In proteins, very distant and small interactions between collections of amino acids provide the communication which can be important for signaling process. In this paper, we present the SCA of protein alignment of the esterase family (pfam ID: PF00756) containing the sequence of antigen 85C secreted by Mycobacterium tuberculosis to identify a subset of interacting residues. Clustering analysis of the pairwise correlation highlighted seven important residue positions in the esterase family alignments. These residues were then mapped on the crystal structure of antigen 85C (PDB ID: 1DQZ). The mapping revealed correlation between 3 distant residues (Asp38, Leu123 and Met125) and suggests allosteric communication between them. This information can be used for a new drug against this fatal disease. Editorial Department of Journal of Biomedical Research 2011-05 /pmc/articles/PMC3597060/ /pubmed/23554685 http://dx.doi.org/10.1016/S1674-8301(11)60021-3 Text en © 2011 by the Journal of Biomedical Research. All rights reserved. This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Research Paper Baths, Veeky Roy, Utpal Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title | Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title_full | Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title_fullStr | Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title_full_unstemmed | Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title_short | Identification of distant co-evolving residues in antigen 85C from Mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
title_sort | identification of distant co-evolving residues in antigen 85c from mycobacterium tuberculosis using statistical coupling analysis of the esterase family proteins |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597060/ https://www.ncbi.nlm.nih.gov/pubmed/23554685 http://dx.doi.org/10.1016/S1674-8301(11)60021-3 |
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