Backbone 1H, 13C, and 15N assignments of the extracellular region of human Fcγ receptor IIIb
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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.
KeywordsFcγ 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.
All experiments outlined here are in compliance with the laws of Japan.
- 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
- 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
- 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
- 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