PMID- 30484251
OWN - NLM
STAT- MEDLINE
DCOM- 20190729
LR  - 20190729
IS  - 0065-2598 (Print)
IS  - 0065-2598 (Linking)
VI  - 1104
DP  - 2018
TI  - Structure and Dynamics of Immunoglobulin G Glycoproteins.
PG  - 219-235
LID - 10.1007/978-981-13-2158-0_11 [doi]
AB  - Immunoglobulin G (IgG) is a major serum glycoprotein that exerts the role of 
      antibody in the immune system. This multifunctional glycoprotein couples antigen 
      recognition with a variety of effector functions promoted via interactions with 
      various IgG-binding proteins. Given its versatile functionality, IgG has recently 
      been used for therapeutic interventions. Evidence indicates that the carbohydrate 
      moieties of IgG glycoproteins critically affect their antibody functions, 
      particularly the effector functions mediated by the interactions with Fcgamma 
      receptors (FcgammaRs). N-glycans at specific positions of FcgammaR also contribute both 
      positively and negatively to the interactions with IgG. The integration of 
      multilateral biophysical approaches, including X-ray crystallography, nuclear 
      magnetic resonance spectroscopy, and molecular dynamics simulations, has provided 
      structural insights into the mechanisms underlying the glycofunctions of this 
      interacting system. The N-glycans of IgG and FcgammaR mediate their interactions by 
      either strengthening or weakening the affinity on the basis of their glycoforms. 
      Moreover, the N-glycosylation of IgG-Fc is a prerequisite to maintain the 
      integrity of the quaternary structure of the sites interacting with the effector 
      molecules and can also control functionally relevant local conformations. The 
      biopharmaceutical significance of these glycan functions is discussed from a 
      structural point of view.
FAU - Yagi, Hirokazu
AU  - Yagi H
AD  - Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, 
      Japan.
FAU - Yanaka, Saeko
AU  - Yanaka S
AD  - Exploratory Research Center on Life and Living Systems (ExCELLS) and Institute 
      for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi, 
      Japan.
FAU - Kato, Koichi
AU  - Kato K
AD  - Exploratory Research Center on Life and Living Systems, National Institutes of 
      Natural Sciences, Okazaki, Aichi, Japan. kkato@phar.nagoya-cu.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Adv Exp Med Biol
JT  - Advances in experimental medicine and biology
JID - 0121103
RN  - 0 (Glycoproteins)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Receptors, IgG)
MH  - Glycoproteins/*chemistry
MH  - *Glycosylation
MH  - Immunoglobulin G/*chemistry
MH  - Protein Binding
MH  - Receptors, IgG/*chemistry
OTO - NOTNLM
OT  - Fcgamma receptor
OT  - Immunoglobulin G
OT  - N-linked oligosaccharide
OT  - Nuclear magnetic resonance spectroscopy
OT  - Stable isotope labeling
OT  - Therapeutic antibody
OT  - X-ray crystallography
EDAT- 2018/11/30 06:00
MHDA- 2019/07/30 06:00
CRDT- 2018/11/29 06:00
PHST- 2018/11/29 06:00 [entrez]
PHST- 2018/11/30 06:00 [pubmed]
PHST- 2019/07/30 06:00 [medline]
AID - 10.1007/978-981-13-2158-0_11 [doi]
PST - ppublish
SO  - Adv Exp Med Biol. 2018;1104:219-235. doi: 10.1007/978-981-13-2158-0_11.