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Yogo R, Yanaka S, Yagi H, et al. Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering. Biochem Biophys Rep. 2017;12:1-4doi: 10.1016/j.bbrep.2017.08.004.
Yogo, R., Yanaka, S., Yagi, H., Martel, A., Porcar, L., Ueki, Y., Inoue, R., Sato, N., Sugiyama, M., & Kato, K. (2017). Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering. Biochemistry and biophysics reports, 121-4. https://doi.org/10.1016/j.bbrep.2017.08.004
Yogo, Rina, et al. "Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering." Biochemistry and biophysics reports vol. 12 (2017): 1-4. doi: https://doi.org/10.1016/j.bbrep.2017.08.004
Yogo R, Yanaka S, Yagi H, Martel A, Porcar L, Ueki Y, Inoue R, Sato N, Sugiyama M, Kato K. Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering. Biochem Biophys Rep. 2017 Aug 16;12:1-4. doi: 10.1016/j.bbrep.2017.08.004. eCollection 2017 Dec. PMID: 28955785; PMCID: PMC5613214.
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Biochem Biophys Rep. 2017 Aug 16;12:1-4. doi: 10.1016/j.bbrep.2017.08.004. eCollection 2017 Dec.

Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering.

Biochemistry and biophysics reports

Rina Yogo, Saeko Yanaka, Hirokazu Yagi, Anne Martel, Linoel Porcar, Yutaro Ueki, Rintaro Inoue, Nobuhiro Sato, Masaaki Sugiyama, Koichi Kato

Affiliations

  1. Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan.
  2. Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuhoku, Nagoya 467-8603, Japan.
  3. Institut Laue-Langevin, 6 Rue Jules Horowitz, Grenoble 38042, France.
  4. Graduate School of Engineering, Kyoto University, Yoshida-honmachi, Sakyo-ku, Kyoto 606-8501, Japan.
  5. Research Reactor Institute, Kyoto University, Kumatori, Sennan-gun, Osaka 590-0494, Japan.

PMID: 28955785 PMCID: PMC5613214 DOI: 10.1016/j.bbrep.2017.08.004

Abstract

A recently developed integrative approach combining varied types of experimental data has been successfully applied to three-dimensional modelling of larger biomacromolecular complexes. Deuteration-assisted small-angle neutron scattering (SANS) plays a unique role in this approach by making it possible to observe selected components in the complex. It enables integrative modelling of biomolecular complexes based on building-block structures typically provided by X-ray crystallography. In this integrative approach, it is important to be aware of the flexible properties of the individual building blocks. Here we examine the ability of SANS to detect a subtle conformational change of a multidomain protein using the Fc portion of human immunoglobulin G (IgG) interacting with a soluble form of the low-affinity Fcγ receptor IIIb (sFcγRIIIb) as a model system. The IgG-Fc glycoprotein was subjected to SANS in the absence and presence of 75%-deuterated sFcγRIIIb, which was matched out in D

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