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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...

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Detalles Bibliográficos
Autores principales: Piovesan, Damiano, Monzon, Alexander Miguel, Quaglia, Federica, Tosatto, Silvio C. E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
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.
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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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