Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein

Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein

The Fc portion of immunoglobulin G (IgG) recruits complements and its cognate receptors, thereby promoting defensive mechanisms in the humoral immune system. These effector functions critically depend on N-glycosylation at the Fc region, which is therefore regarded as a crucial factor in the design...

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Main Authors: Yagi, Hirokazu, Zhang, Ying, Yagi-Utsumi, Maho, Yamaguchi, Takumi, Iida, Shigeru, Yamaguchi, Yoshiki, Kato, Koichi
Format: Online
Language:English
Published: Springer Netherlands 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568019/
id pubmed-4568019
recordtype oai_dc
spelling pubmed-45680192015-09-15 Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein Yagi, Hirokazu Zhang, Ying Yagi-Utsumi, Maho Yamaguchi, Takumi Iida, Shigeru Yamaguchi, Yoshiki Kato, Koichi Article The Fc portion of immunoglobulin G (IgG) recruits complements and its cognate receptors, thereby promoting defensive mechanisms in the humoral immune system. These effector functions critically depend on N-glycosylation at the Fc region, which is therefore regarded as a crucial factor in the design and production of therapeutic antibodies. NMR spectroscopy plays a unique role in the characterization of conformational dynamics and intermolecular interactions of IgG-Fc in solutions. Here, we report NMR assignments of the glycosylated Fc fragment (Mr 53 kDa), cleaved from a chimeric antibody with human IgG1 constant regions, which was produced in Chinese hamster ovary cells with uniform 13C- and 15N-labeling. Springer Netherlands 2014-10-08 2015 /pmc/articles/PMC4568019/ /pubmed/25291979 http://dx.doi.org/10.1007/s12104-014-9586-7 Text en © The Author(s) 2014 Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Yagi, Hirokazu
Zhang, Ying
Yagi-Utsumi, Maho
Yamaguchi, Takumi
Iida, Shigeru
Yamaguchi, Yoshiki
Kato, Koichi
spellingShingle Yagi, Hirokazu
Zhang, Ying
Yagi-Utsumi, Maho
Yamaguchi, Takumi
Iida, Shigeru
Yamaguchi, Yoshiki
Kato, Koichi
Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
author_facet Yagi, Hirokazu
Zhang, Ying
Yagi-Utsumi, Maho
Yamaguchi, Takumi
Iida, Shigeru
Yamaguchi, Yoshiki
Kato, Koichi
author_sort Yagi, Hirokazu
title Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
title_short Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
title_full Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
title_fullStr Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
title_full_unstemmed Backbone 1H, 13C, and 15N resonance assignments of the Fc fragment of human immunoglobulin G glycoprotein
title_sort backbone 1h, 13c, and 15n resonance assignments of the fc fragment of human immunoglobulin g glycoprotein
description The Fc portion of immunoglobulin G (IgG) recruits complements and its cognate receptors, thereby promoting defensive mechanisms in the humoral immune system. These effector functions critically depend on N-glycosylation at the Fc region, which is therefore regarded as a crucial factor in the design and production of therapeutic antibodies. NMR spectroscopy plays a unique role in the characterization of conformational dynamics and intermolecular interactions of IgG-Fc in solutions. Here, we report NMR assignments of the glycosylated Fc fragment (Mr 53 kDa), cleaved from a chimeric antibody with human IgG1 constant regions, which was produced in Chinese hamster ovary cells with uniform 13C- and 15N-labeling.
publisher Springer Netherlands
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568019/
_version_ 1613475186812649472

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