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PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins

Posttranslational modifications (PTMs) define covalent and chemical modifications of protein residues. They play important roles in modulating various biological functions. Current PTM databases contain important sequence annotations but do not provide informative 3D structural resource about these...

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Detalles Bibliográficos
Autores principales: Craveur, Pierrick, Rebehmed, Joseph, de Brevern, Alexandre G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4038255/
https://www.ncbi.nlm.nih.gov/pubmed/24857970
http://dx.doi.org/10.1093/database/bau041
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author Craveur, Pierrick
Rebehmed, Joseph
de Brevern, Alexandre G.
author_facet Craveur, Pierrick
Rebehmed, Joseph
de Brevern, Alexandre G.
author_sort Craveur, Pierrick
collection PubMed
description Posttranslational modifications (PTMs) define covalent and chemical modifications of protein residues. They play important roles in modulating various biological functions. Current PTM databases contain important sequence annotations but do not provide informative 3D structural resource about these modifications. Posttranslational modification structural database (PTM-SD) provides access to structurally solved modified residues, which are experimentally annotated as PTMs. It combines different PTM information and annotation gathered from other databases, e.g. Protein DataBank for the protein structures and dbPTM and PTMCuration for fine sequence annotation. PTM-SD gives an accurate detection of PTMs in structural data. PTM-SD can be browsed by PDB id, UniProt accession number, organism and classic PTM annotation. Advanced queries can also be performed, i.e. detailed PTM annotations, amino acid type, secondary structure, SCOP class classification, PDB chain length and number of PTMs by chain. Statistics and analyses can be computed on a selected dataset of PTMs. Each PTM entry is detailed in a dedicated page with information on the protein sequence, local conformation with secondary structure and Protein Blocks. PTM-SD gives valuable information on observed PTMs in protein 3D structure, which is of great interest for studying sequence–structure– function relationships at the light of PTMs, and could provide insights for comparative modeling and PTM predictions protocols. Database URL: PTM-SD can be accessed at http://www.dsimb.inserm.fr/dsimb_tools/PTM-SD/.
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spelling pubmed-40382552014-06-18 PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins Craveur, Pierrick Rebehmed, Joseph de Brevern, Alexandre G. Database (Oxford) Original Article Posttranslational modifications (PTMs) define covalent and chemical modifications of protein residues. They play important roles in modulating various biological functions. Current PTM databases contain important sequence annotations but do not provide informative 3D structural resource about these modifications. Posttranslational modification structural database (PTM-SD) provides access to structurally solved modified residues, which are experimentally annotated as PTMs. It combines different PTM information and annotation gathered from other databases, e.g. Protein DataBank for the protein structures and dbPTM and PTMCuration for fine sequence annotation. PTM-SD gives an accurate detection of PTMs in structural data. PTM-SD can be browsed by PDB id, UniProt accession number, organism and classic PTM annotation. Advanced queries can also be performed, i.e. detailed PTM annotations, amino acid type, secondary structure, SCOP class classification, PDB chain length and number of PTMs by chain. Statistics and analyses can be computed on a selected dataset of PTMs. Each PTM entry is detailed in a dedicated page with information on the protein sequence, local conformation with secondary structure and Protein Blocks. PTM-SD gives valuable information on observed PTMs in protein 3D structure, which is of great interest for studying sequence–structure– function relationships at the light of PTMs, and could provide insights for comparative modeling and PTM predictions protocols. Database URL: PTM-SD can be accessed at http://www.dsimb.inserm.fr/dsimb_tools/PTM-SD/. Oxford University Press 2014-05-24 /pmc/articles/PMC4038255/ /pubmed/24857970 http://dx.doi.org/10.1093/database/bau041 Text en © The Author(s) 2014. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Craveur, Pierrick
Rebehmed, Joseph
de Brevern, Alexandre G.
PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title_full PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title_fullStr PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title_full_unstemmed PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title_short PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins
title_sort ptm-sd: a database of structurally resolved and annotated posttranslational modifications in proteins
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4038255/
https://www.ncbi.nlm.nih.gov/pubmed/24857970
http://dx.doi.org/10.1093/database/bau041
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