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Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL
Protein–carbohydrate interactions are very often mediated by the stacking CH–π interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp s...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726637/ https://www.ncbi.nlm.nih.gov/pubmed/29232414 http://dx.doi.org/10.1371/journal.pone.0189375 |
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author | Houser, Josef Kozmon, Stanislav Mishra, Deepti Mishra, Sushil K. Romano, Patrick R. Wimmerová, Michaela Koča, Jaroslav |
author_facet | Houser, Josef Kozmon, Stanislav Mishra, Deepti Mishra, Sushil K. Romano, Patrick R. Wimmerová, Michaela Koča, Jaroslav |
author_sort | Houser, Josef |
collection | PubMed |
description | Protein–carbohydrate interactions are very often mediated by the stacking CH–π interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate like ligands in 5 208 Trp containing motives. An appropriate model system to study such an interaction is the AAL lectin family where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with α-methyl-l-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp–carbohydrate complexes, which would suggest no substantial preference for one conformation over another. |
format | Online Article Text |
id | pubmed-5726637 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57266372017-12-22 Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL Houser, Josef Kozmon, Stanislav Mishra, Deepti Mishra, Sushil K. Romano, Patrick R. Wimmerová, Michaela Koča, Jaroslav PLoS One Research Article Protein–carbohydrate interactions are very often mediated by the stacking CH–π interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate like ligands in 5 208 Trp containing motives. An appropriate model system to study such an interaction is the AAL lectin family where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with α-methyl-l-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp–carbohydrate complexes, which would suggest no substantial preference for one conformation over another. Public Library of Science 2017-12-12 /pmc/articles/PMC5726637/ /pubmed/29232414 http://dx.doi.org/10.1371/journal.pone.0189375 Text en © 2017 Houser et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Houser, Josef Kozmon, Stanislav Mishra, Deepti Mishra, Sushil K. Romano, Patrick R. Wimmerová, Michaela Koča, Jaroslav Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title | Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title_full | Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title_fullStr | Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title_full_unstemmed | Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title_short | Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL |
title_sort | influence of trp flipping on carbohydrate binding in lectins. an example on aleuria aurantia lectin aal |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726637/ https://www.ncbi.nlm.nih.gov/pubmed/29232414 http://dx.doi.org/10.1371/journal.pone.0189375 |
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