Cargando…

Making glycoproteins a little bit sweeter with PDB-REDO

Glycosylation is one of the most common forms of protein post-translational modification, but is also the most complex. Dealing with glycoproteins in structure model building, refinement, validation and PDB deposition is more error-prone than dealing with nonglycosylated proteins owing to limitation...

Descripción completa

Detalles Bibliográficos
Autores principales: van Beusekom, Bart, Lütteke, Thomas, Joosten, Robbie P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6096482/
https://www.ncbi.nlm.nih.gov/pubmed/30084395
http://dx.doi.org/10.1107/S2053230X18004016
_version_ 1783348109655408640
author van Beusekom, Bart
Lütteke, Thomas
Joosten, Robbie P.
author_facet van Beusekom, Bart
Lütteke, Thomas
Joosten, Robbie P.
author_sort van Beusekom, Bart
collection PubMed
description Glycosylation is one of the most common forms of protein post-translational modification, but is also the most complex. Dealing with glycoproteins in structure model building, refinement, validation and PDB deposition is more error-prone than dealing with nonglycosylated proteins owing to limitations of the experimental data and available software tools. Also, experimentalists are typically less experienced in dealing with carbohydrate residues than with amino-acid residues. The results of the reannotation and re-refinement by PDB-REDO of 8114 glycoprotein structure models from the Protein Data Bank are analyzed. The positive aspects of 3620 reannotations and subsequent refinement, as well as the remaining challenges to obtaining consistently high-quality carbohydrate models, are discussed.
format Online
Article
Text
id pubmed-6096482
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher International Union of Crystallography
record_format MEDLINE/PubMed
spelling pubmed-60964822018-08-24 Making glycoproteins a little bit sweeter with PDB-REDO van Beusekom, Bart Lütteke, Thomas Joosten, Robbie P. Acta Crystallogr F Struct Biol Commun Research Communications Glycosylation is one of the most common forms of protein post-translational modification, but is also the most complex. Dealing with glycoproteins in structure model building, refinement, validation and PDB deposition is more error-prone than dealing with nonglycosylated proteins owing to limitations of the experimental data and available software tools. Also, experimentalists are typically less experienced in dealing with carbohydrate residues than with amino-acid residues. The results of the reannotation and re-refinement by PDB-REDO of 8114 glycoprotein structure models from the Protein Data Bank are analyzed. The positive aspects of 3620 reannotations and subsequent refinement, as well as the remaining challenges to obtaining consistently high-quality carbohydrate models, are discussed. International Union of Crystallography 2018-07-26 /pmc/articles/PMC6096482/ /pubmed/30084395 http://dx.doi.org/10.1107/S2053230X18004016 Text en © van Beusekom et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ 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.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Communications
van Beusekom, Bart
Lütteke, Thomas
Joosten, Robbie P.
Making glycoproteins a little bit sweeter with PDB-REDO
title Making glycoproteins a little bit sweeter with PDB-REDO
title_full Making glycoproteins a little bit sweeter with PDB-REDO
title_fullStr Making glycoproteins a little bit sweeter with PDB-REDO
title_full_unstemmed Making glycoproteins a little bit sweeter with PDB-REDO
title_short Making glycoproteins a little bit sweeter with PDB-REDO
title_sort making glycoproteins a little bit sweeter with pdb-redo
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6096482/
https://www.ncbi.nlm.nih.gov/pubmed/30084395
http://dx.doi.org/10.1107/S2053230X18004016
work_keys_str_mv AT vanbeusekombart makingglycoproteinsalittlebitsweeterwithpdbredo
AT luttekethomas makingglycoproteinsalittlebitsweeterwithpdbredo
AT joostenrobbiep makingglycoproteinsalittlebitsweeterwithpdbredo