Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

AlfC transfucosidase is used to modulate fucosylation of glycans decorating monoclonal antibodies. Herein, structural and biophysical characterization reveals the enzymatic mechanism of AlfC and a blueprint for the design of AlfC mutants with novel specificities and functions.

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Autores principales:	Erik H. Klontz, Chao Li, Kyle Kihn, James K. Fields, Dorothy Beckett, Greg A. Snyder, Patrick L. Wintrode, Daniel Deredge, Lai-Xi Wang, Eric J. Sundberg
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9a30450512214f37b47bbcf6f541a3c3
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spelling	oai:doaj.org-article:9a30450512214f37b47bbcf6f541a3c32021-12-02T16:49:28ZStructure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation10.1038/s41467-020-20044-z2041-1723https://doaj.org/article/9a30450512214f37b47bbcf6f541a3c32020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20044-zhttps://doaj.org/toc/2041-1723AlfC transfucosidase is used to modulate fucosylation of glycans decorating monoclonal antibodies. Herein, structural and biophysical characterization reveals the enzymatic mechanism of AlfC and a blueprint for the design of AlfC mutants with novel specificities and functions.Erik H. KlontzChao LiKyle KihnJames K. FieldsDorothy BeckettGreg A. SnyderPatrick L. WintrodeDaniel DeredgeLai-Xi WangEric J. SundbergNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Erik H. Klontz Chao Li Kyle Kihn James K. Fields Dorothy Beckett Greg A. Snyder Patrick L. Wintrode Daniel Deredge Lai-Xi Wang Eric J. Sundberg Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
description	AlfC transfucosidase is used to modulate fucosylation of glycans decorating monoclonal antibodies. Herein, structural and biophysical characterization reveals the enzymatic mechanism of AlfC and a blueprint for the design of AlfC mutants with novel specificities and functions.
format	article
author	Erik H. Klontz Chao Li Kyle Kihn James K. Fields Dorothy Beckett Greg A. Snyder Patrick L. Wintrode Daniel Deredge Lai-Xi Wang Eric J. Sundberg
author_facet	Erik H. Klontz Chao Li Kyle Kihn James K. Fields Dorothy Beckett Greg A. Snyder Patrick L. Wintrode Daniel Deredge Lai-Xi Wang Eric J. Sundberg
author_sort	Erik H. Klontz
title	Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
title_short	Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
title_full	Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
title_fullStr	Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
title_full_unstemmed	Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation
title_sort	structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient igg transfucosylation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/9a30450512214f37b47bbcf6f541a3c3
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Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

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