PMID- 32410186
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20240329
IS  - 1867-2450 (Print)
IS  - 1867-2469 (Electronic)
IS  - 1867-2450 (Linking)
VI  - 12
IP  - 3
DP  - 2020 Jun
TI  - Biophysical characterization of dynamic structures of immunoglobulin G.
PG  - 637-645
LID - 10.1007/s12551-020-00698-1 [doi]
AB  - Immunoglobulin G (IgG) is a major antibody and functions as a hub linking 
      specific antigen binding and recruitment of effector molecules typified by Fcgamma 
      receptors (FcgammaRs). These activities are associated primarily with interactions 
      involving its Fab and Fc sites, respectively. An IgG molecule is characterized by 
      a multiple domain modular structure with conserved N-glycosylation in Fc. The 
      molecule displays significant freedom in internal motion on various 
      spatiotemporal scales. The consequent conformational flexibility and plasticity 
      of IgG glycoproteins are functionally significant and potentially important 
      factors for design and engineering of antibodies with enhanced functionality. In 
      this article, experimental and computational approaches are outlined for 
      characterizing the conformational dynamics of IgG molecules in solution. In 
      particular, the importance of integration of these approaches is highlighted, as 
      illustrated by dynamic intramolecular interactions between the pair of N-glycans 
      and their proximal amino acid residues in Fc. These interactions can critically 
      affect effector functions mediated by human IgG1 and FcgammaRIII. Further 
      improvements in individual biophysical techniques and their integration will 
      advance understanding of dynamic behaviors of antibodies in physiological and 
      pathological conditions. Such understanding will provide opportunities for 
      engineering antibodies through controlling allosteric networks in IgG molecules.
FAU - Yanaka, Saeko
AU  - Yanaka S
AUID- ORCID: 0000-0002-3513-5701
AD  - Exploratory Research Center on Life and Living Systems (ExCELLS) and Institute 
      for Molecular Science (IMS), National Institutes of Natural Sciences, 5-1 
      Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
AD  - Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 
      Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan.
FAU - Yogo, Rina
AU  - Yogo R
AUID- ORCID: 0000-0002-1595-0194
AD  - Exploratory Research Center on Life and Living Systems (ExCELLS) and Institute 
      for Molecular Science (IMS), National Institutes of Natural Sciences, 5-1 
      Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
AD  - Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 
      Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan.
FAU - Kato, Koichi
AU  - Kato K
AUID- ORCID: 0000-0001-7187-9612
AD  - Exploratory Research Center on Life and Living Systems (ExCELLS) and Institute 
      for Molecular Science (IMS), National Institutes of Natural Sciences, 5-1 
      Higashiyama, Myodaiji, Okazaki, 444-8787, Japan. kkatonmr@ims.ac.jp.
AD  - Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 
      Tanabe-dori, Mizuho-ku, Nagoya, Aichi, 467-8603, Japan. kkatonmr@ims.ac.jp.
LA  - eng
GR  - JP18K14892/Ministry of Education Culture Sports Science and Technology/
GR  - JP19J15602/Ministry of Education Culture Sports Science and Technology/
GR  - JP19H01017/Ministry of Education Culture Sports Science and Technology/
PT  - Journal Article
PT  - Review
DEP - 20200515
PL  - Germany
TA  - Biophys Rev
JT  - Biophysical reviews
JID - 101498573
PMC - PMC7311591
OTO - NOTNLM
OT  - Antibody
OT  - Core fucosylation
OT  - Dynamic conformational ensemble
OT  - Fcgamma receptor
OT  - Immunoglobulin G
OT  - Molecular dynamics simulation
OT  - N-glycan
OT  - Nuclear magnetic resonance spectroscopy
OT  - Solution scattering
OT  - X-ray crystallography
EDAT- 2020/05/16 06:00
MHDA- 2020/05/16 06:01
PMCR- 2020/05/15
CRDT- 2020/05/16 06:00
PHST- 2020/03/07 00:00 [received]
PHST- 2020/05/01 00:00 [accepted]
PHST- 2020/05/16 06:00 [pubmed]
PHST- 2020/05/16 06:01 [medline]
PHST- 2020/05/16 06:00 [entrez]
PHST- 2020/05/15 00:00 [pmc-release]
AID - 10.1007/s12551-020-00698-1 [pii]
AID - 698 [pii]
AID - 10.1007/s12551-020-00698-1 [doi]
PST - ppublish
SO  - Biophys Rev. 2020 Jun;12(3):637-645. doi: 10.1007/s12551-020-00698-1. Epub 2020 
      May 15.