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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2018
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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 |
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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
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title_full | Making glycoproteins a little bit sweeter with PDB-REDO
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title_fullStr | Making glycoproteins a little bit sweeter with PDB-REDO
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title_full_unstemmed | Making glycoproteins a little bit sweeter with PDB-REDO
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title_short | Making glycoproteins a little bit sweeter with PDB-REDO
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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 |
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