Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 201–204 | Cite as

Backbone 1H, 13C, and 15N assignments of the extracellular region of human Fcγ receptor IIIb

  • Rina Yogo
  • Saeko Yanaka
  • Koichi Kato


Fcγ receptor (FcγR) promotes various immune responses through interactions with the Fc portion of immunoglobulin G (IgG). FcγRIIIb is a glycosylphosphatidylinositol-linked protein expressed on neutrophils and triggers degranulation and opsonic phagocytosis. The extracellular region of FcγR is composed of two Ig-fold domains and can be cleaved as a soluble form (sFcγRIIIb), which is also reactive with complement receptor type 3. Although structure and Fc interaction of sFcγRIIIb have been characterized by X-ray crystallography, little has been known about its structure in solution. We herein report the backbone NMR assignments of human sFcγRIIIb to gain basic understanding of functional IgG–FcγRIII interactions of immunological and biopharmaceutical interest regarding the structural investigation.


Fcγ receptor Immunoglobulin G NMR spectroscopy Resonance assignment 



We thank Drs. Hirokazu Yagi, Tadashi Satoh (Nagoya City University), and Takahisa Ikegami (Yokohama City University) for useful discussion. We thank Dr. Yohei Miyanoiri (Osaka University) for help in NMR data acquisition. This work was partly supported by the Nanotechnology Platform Program (Molecule and Material Synthesis) of MEXT, MEXT/JSPS Grants in Aid for Scientific Research (JP25102008 and JP17H05893), and the Cooperative Research Program of Institute for Protein Research, Osaka University, NMRCR-16-05.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

All experiments outlined here are in compliance with the laws of Japan.


  1. Bruhns P (2012) Properties of mouse and human IgG receptors and their contribution to disease models. Blood 119:5640–5649CrossRefGoogle Scholar
  2. Bruhns P, Iannascoli B, England P, Mancardi DA, Fernandez N, Jorieux S, Daëron M (2009) Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses. Blood 113:3716–3725CrossRefGoogle Scholar
  3. Daëron M (1997) Fc receptor biology. Annu Rev Immunol 15:203–234CrossRefGoogle Scholar
  4. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) Nmrpipe: a multidimensional spectral processing system based on Unix Pipes. J Biomol NMR 6:277–293CrossRefGoogle Scholar
  5. Galon J, Gauchat JF, Maziéres N, Spagnoli R, Storkus W, Lötze M, Bonnefoy JY, Fridman WH, Sautés C (1996) Soluble Fc gamma receptor type III (Fc gamma RIII, CD16) triggers cell activation through interaction with complement receptors. J Immunol 157:1184–1192Google Scholar
  6. Gillis C, Gouel-Chéron A, Jönsson F, Bruhns P (2014) Contribution of human FcγRs to disease with evidence from human polymorphisms and transgenic animal studies. Front Immunol 5:254CrossRefGoogle Scholar
  7. Hafsa NE, Arndt D, Wishart DS (2015) CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts. Nucleic Acids Res 43:W370-W377CrossRefGoogle Scholar
  8. Hayes JM, Wormald MR, Rudd PM, Davey GP (2016) Fc gamma receptors: glycobiology and therapeutic prospects. J Inflamm Res 9:209–219CrossRefGoogle Scholar
  9. Kobayashi N, Iwahara J, Koshiba S, Tomizawa T, Tochio N, Güntert P, Kigawa T, Yokoyama S (2007) KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. J Biomol NMR 39:31–52CrossRefGoogle Scholar
  10. Kobayashi N, Harano Y, Tochio N, Nakatani E, Kigawa T, Yokoyama S, Mading S, Ulrich EL, Markley JL, Akutsu H, Fujiwara T (2012) An automated system designed for large scale NMR data deposition and annotation: application to over 600 assigned chemical shift data entries to the BioMagResBank from the riken structural genomics/proteomics initiative internal database. J Biomol NMR 53:311–320CrossRefGoogle Scholar
  11. Radaev S, Motyka S, Fridman WH, Sautes-Fridman C, Sun PD (2001) The structure of a human type III Fcγ receptor in complex with Fc. J Biol Chem 276:16469–16477CrossRefGoogle Scholar
  12. Sondermann P, Huber R, Oosthuizen V, Jacob U (2000) The 3.2-A crystal structure of the human IgG1 Fc fragment-FcγRIII complex. Nature 406:267–273ADSCrossRefGoogle Scholar
  13. Yagi-Utsumi M, Matsuo K, Yanagisawa K, Gekko K, Kato K (2010) Spectroscopic characterization of intermolecular interaction of amyloid β promoted on GM1 micelles. Int J Alzheimers Dis 2011:925073Google Scholar
  14. 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. Biochem Biophys Rep 12:1–4Google Scholar
  15. Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD (2000) Crystal structure of the extracellular domain of a human FcγRIII. Immunity 13:387–395CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  1. 1.Institute for Molecular Science and Okazaki Institute for Integrative BioscienceNational Institutes of Natural SciencesOkazakiJapan
  2. 2.Graduate School of Pharmaceutical SciencesNagoya City UniversityNagoyaJapan

Personalised recommendations