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Databases for intrinsically disordered proteins
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8805306/ https://www.ncbi.nlm.nih.gov/pubmed/35102880 http://dx.doi.org/10.1107/S2059798321012109 |
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author | Piovesan, Damiano Monzon, Alexander Miguel Quaglia, Federica Tosatto, Silvio C. E. |
author_facet | Piovesan, Damiano Monzon, Alexander Miguel Quaglia, Federica Tosatto, Silvio C. E. |
author_sort | Piovesan, Damiano |
collection | PubMed |
description | Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature. Predictions of IDRs are still difficult to estimate and are poorly characterized. Here, an overview of the publicly available knowledge about IDRs is reported, including manually curated resources, deposition databases and prediction repositories. The types, scopes and availability of the various resources are analyzed, and their complementarity and overlap are highlighted. The volume of information included and the relevance to the field of structural biology are compared. |
format | Online Article Text |
id | pubmed-8805306 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-88053062022-02-09 Databases for intrinsically disordered proteins Piovesan, Damiano Monzon, Alexander Miguel Quaglia, Federica Tosatto, Silvio C. E. Acta Crystallogr D Struct Biol Ccp4 Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature. Predictions of IDRs are still difficult to estimate and are poorly characterized. Here, an overview of the publicly available knowledge about IDRs is reported, including manually curated resources, deposition databases and prediction repositories. The types, scopes and availability of the various resources are analyzed, and their complementarity and overlap are highlighted. The volume of information included and the relevance to the field of structural biology are compared. International Union of Crystallography 2022-01-21 /pmc/articles/PMC8805306/ /pubmed/35102880 http://dx.doi.org/10.1107/S2059798321012109 Text en © Damiano Piovesan et al. 2022 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Ccp4 Piovesan, Damiano Monzon, Alexander Miguel Quaglia, Federica Tosatto, Silvio C. E. Databases for intrinsically disordered proteins |
title | Databases for intrinsically disordered proteins |
title_full | Databases for intrinsically disordered proteins |
title_fullStr | Databases for intrinsically disordered proteins |
title_full_unstemmed | Databases for intrinsically disordered proteins |
title_short | Databases for intrinsically disordered proteins |
title_sort | databases for intrinsically disordered proteins |
topic | Ccp4 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8805306/ https://www.ncbi.nlm.nih.gov/pubmed/35102880 http://dx.doi.org/10.1107/S2059798321012109 |
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