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3did: identification and classification of domain-based interactions of known three-dimensional structure

The database of three-dimensional interacting domains (3did) is a collection of protein interactions for which high-resolution three-dimensional structures are known. 3did exploits the availability of structural data to provide molecular details on interactions between two globular domains as well a...

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Detalles Bibliográficos
Autores principales: Stein, Amelie, Céol, Arnaud, Aloy, Patrick
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013799/
https://www.ncbi.nlm.nih.gov/pubmed/20965963
http://dx.doi.org/10.1093/nar/gkq962
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author Stein, Amelie
Céol, Arnaud
Aloy, Patrick
author_facet Stein, Amelie
Céol, Arnaud
Aloy, Patrick
author_sort Stein, Amelie
collection PubMed
description The database of three-dimensional interacting domains (3did) is a collection of protein interactions for which high-resolution three-dimensional structures are known. 3did exploits the availability of structural data to provide molecular details on interactions between two globular domains as well as novel domain–peptide interactions, derived using a recently published method from our lab. The interface residues are presented for each interaction type individually, plus global domain interfaces at which one or more partners (domains or peptides) bind. The 3did web server at http://3did.irbbarcelona.org visualizes these interfaces along with atomic details of individual interactions using Jmol. The complete contents are also available for download.
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spelling pubmed-30137992011-01-03 3did: identification and classification of domain-based interactions of known three-dimensional structure Stein, Amelie Céol, Arnaud Aloy, Patrick Nucleic Acids Res Articles The database of three-dimensional interacting domains (3did) is a collection of protein interactions for which high-resolution three-dimensional structures are known. 3did exploits the availability of structural data to provide molecular details on interactions between two globular domains as well as novel domain–peptide interactions, derived using a recently published method from our lab. The interface residues are presented for each interaction type individually, plus global domain interfaces at which one or more partners (domains or peptides) bind. The 3did web server at http://3did.irbbarcelona.org visualizes these interfaces along with atomic details of individual interactions using Jmol. The complete contents are also available for download. Oxford University Press 2011-01 2010-10-21 /pmc/articles/PMC3013799/ /pubmed/20965963 http://dx.doi.org/10.1093/nar/gkq962 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Stein, Amelie
Céol, Arnaud
Aloy, Patrick
3did: identification and classification of domain-based interactions of known three-dimensional structure
title 3did: identification and classification of domain-based interactions of known three-dimensional structure
title_full 3did: identification and classification of domain-based interactions of known three-dimensional structure
title_fullStr 3did: identification and classification of domain-based interactions of known three-dimensional structure
title_full_unstemmed 3did: identification and classification of domain-based interactions of known three-dimensional structure
title_short 3did: identification and classification of domain-based interactions of known three-dimensional structure
title_sort 3did: identification and classification of domain-based interactions of known three-dimensional structure
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013799/
https://www.ncbi.nlm.nih.gov/pubmed/20965963
http://dx.doi.org/10.1093/nar/gkq962
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