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IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures
BACKGROUND: Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes. Intrinsically disordered proteins perform various biological functions by interacting with other ligands. RESULTS: Here,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9327236/ https://www.ncbi.nlm.nih.gov/pubmed/35883018 http://dx.doi.org/10.1186/s12860-022-00434-5 |
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author | Sun, CanZhuang Feng, YongE Fan, GuoLiang |
author_facet | Sun, CanZhuang Feng, YongE Fan, GuoLiang |
author_sort | Sun, CanZhuang |
collection | PubMed |
description | BACKGROUND: Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes. Intrinsically disordered proteins perform various biological functions by interacting with other ligands. RESULTS: Here, we present a database, IDPsBind, which displays interacting sites between IDPs and interacting ligands by using the distance threshold method in known 3D structure IDPs complexes from the PDB database. IDPsBind contains 9626 IDPs complexes and 880 intrinsically disordered proteins verified by experiments. The current release of the IDPsBind database is defined as version 1.0. IDPsBind is freely accessible at http://www.s-bioinformatics.cn/idpsbind/home/. CONCLUSIONS: IDPsBind provides more comprehensive interaction sites for IDPs complexes of known 3D structures. It can not only help the subsequent studies of the interaction mechanism of intrinsically disordered proteins but also provides a suitable background for developing the algorithms for predicting the interaction sites of intrinsically disordered proteins. |
format | Online Article Text |
id | pubmed-9327236 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-93272362022-07-28 IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures Sun, CanZhuang Feng, YongE Fan, GuoLiang BMC Mol Cell Biol Database BACKGROUND: Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes. Intrinsically disordered proteins perform various biological functions by interacting with other ligands. RESULTS: Here, we present a database, IDPsBind, which displays interacting sites between IDPs and interacting ligands by using the distance threshold method in known 3D structure IDPs complexes from the PDB database. IDPsBind contains 9626 IDPs complexes and 880 intrinsically disordered proteins verified by experiments. The current release of the IDPsBind database is defined as version 1.0. IDPsBind is freely accessible at http://www.s-bioinformatics.cn/idpsbind/home/. CONCLUSIONS: IDPsBind provides more comprehensive interaction sites for IDPs complexes of known 3D structures. It can not only help the subsequent studies of the interaction mechanism of intrinsically disordered proteins but also provides a suitable background for developing the algorithms for predicting the interaction sites of intrinsically disordered proteins. BioMed Central 2022-07-26 /pmc/articles/PMC9327236/ /pubmed/35883018 http://dx.doi.org/10.1186/s12860-022-00434-5 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Database Sun, CanZhuang Feng, YongE Fan, GuoLiang IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title | IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title_full | IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title_fullStr | IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title_full_unstemmed | IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title_short | IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures |
title_sort | idpsbind: a repository of binding sites for intrinsically disordered proteins complexes with known 3d structures |
topic | Database |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9327236/ https://www.ncbi.nlm.nih.gov/pubmed/35883018 http://dx.doi.org/10.1186/s12860-022-00434-5 |
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