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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...

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Autores principales: 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
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
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 .
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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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