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DisProt: the Database of Disordered Proteins
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We...
Autores principales: | , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1751543/ https://www.ncbi.nlm.nih.gov/pubmed/17145717 http://dx.doi.org/10.1093/nar/gkl893 |
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author | Sickmeier, Megan Hamilton, Justin A. LeGall, Tanguy Vacic, Vladimir Cortese, Marc S. Tantos, Agnes Szabo, Beata Tompa, Peter Chen, Jake Uversky, Vladimir N. Obradovic, Zoran Dunker, A. Keith |
author_facet | Sickmeier, Megan Hamilton, Justin A. LeGall, Tanguy Vacic, Vladimir Cortese, Marc S. Tantos, Agnes Szabo, Beata Tompa, Peter Chen, Jake Uversky, Vladimir N. Obradovic, Zoran Dunker, A. Keith |
author_sort | Sickmeier, Megan |
collection | PubMed |
description | The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at . |
format | Text |
id | pubmed-1751543 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-17515432007-02-22 DisProt: the Database of Disordered Proteins Sickmeier, Megan Hamilton, Justin A. LeGall, Tanguy Vacic, Vladimir Cortese, Marc S. Tantos, Agnes Szabo, Beata Tompa, Peter Chen, Jake Uversky, Vladimir N. Obradovic, Zoran Dunker, A. Keith Nucleic Acids Res Articles The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at . Oxford University Press 2007-01 2006-12-01 /pmc/articles/PMC1751543/ /pubmed/17145717 http://dx.doi.org/10.1093/nar/gkl893 Text en © 2006 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Sickmeier, Megan Hamilton, Justin A. LeGall, Tanguy Vacic, Vladimir Cortese, Marc S. Tantos, Agnes Szabo, Beata Tompa, Peter Chen, Jake Uversky, Vladimir N. Obradovic, Zoran Dunker, A. Keith DisProt: the Database of Disordered Proteins |
title | DisProt: the Database of Disordered Proteins |
title_full | DisProt: the Database of Disordered Proteins |
title_fullStr | DisProt: the Database of Disordered Proteins |
title_full_unstemmed | DisProt: the Database of Disordered Proteins |
title_short | DisProt: the Database of Disordered Proteins |
title_sort | disprot: the database of disordered proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1751543/ https://www.ncbi.nlm.nih.gov/pubmed/17145717 http://dx.doi.org/10.1093/nar/gkl893 |
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